data_9J1B
# 
_entry.id   9J1B 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9J1B         pdb_00009j1b 10.2210/pdb9j1b/pdb 
WWPDB D_1300050149 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-12-04 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9J1B 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-04 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              guosong@fudan.edu.cn 
_pdbx_contact_author.name_first         Guosong 
_pdbx_contact_author.name_last          Chen 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7089-911X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li, L.'   1 ? 
'Chen, G.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Structure of ConA/IMI-Man' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Li, L.'   1 ? 
primary 'Chen, G.' 2 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     nat Concanavalin-A 25622.385 2  ? ? ? ? 
2 non-polymer syn 'MANGANESE (II) ION' 54.938    2  ? ? ? ? 
3 non-polymer syn 'CALCIUM ION' 40.078    2  ? ? ? ? 
4 non-polymer syn 
;~{N}-[2-[(2~{S},3~{S},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxyethyl]-4-[3-[4-[2-[(2~{S},3~{S},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxyethylcarbamoyl]phenyl]imidazol-3-ium-1-yl]benzamide
;
719.713   1  ? ? ? ? 
5 water       nat water 18.015    15 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Con A' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;ADTIVAVELDTYPNTDIGDPSYPHIGIDIKSVRSKKTAKWNMQNGKVGTAHIIYNSVDKRLSAVVSYPNADSATVSYDVD
LDNVLPEWVRVGLSASTGLYKETNTILSWSFTSKLKSNSTHETNALHFMFNQFSKDQKDLILQGDATTGTDGNLELTRVS
SNGSPQGSSVGRALFYAPVHIWESSAVVASFEATFTFLIKSPDSHPADGIAFFISNIDSSIPSGSTGRLLGLFPDAN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ADTIVAVELDTYPNTDIGDPSYPHIGIDIKSVRSKKTAKWNMQNGKVGTAHIIYNSVDKRLSAVVSYPNADSATVSYDVD
LDNVLPEWVRVGLSASTGLYKETNTILSWSFTSKLKSNSTHETNALHFMFNQFSKDQKDLILQGDATTGTDGNLELTRVS
SNGSPQGSSVGRALFYAPVHIWESSAVVASFEATFTFLIKSPDSHPADGIAFFISNIDSSIPSGSTGRLLGLFPDAN
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'MANGANESE (II) ION' MN    
3 'CALCIUM ION' CA    
4 
;~{N}-[2-[(2~{S},3~{S},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxyethyl]-4-[3-[4-[2-[(2~{S},3~{S},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxyethylcarbamoyl]phenyl]imidazol-3-ium-1-yl]benzamide
;
A1EAT 
5 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   ASP n 
1 3   THR n 
1 4   ILE n 
1 5   VAL n 
1 6   ALA n 
1 7   VAL n 
1 8   GLU n 
1 9   LEU n 
1 10  ASP n 
1 11  THR n 
1 12  TYR n 
1 13  PRO n 
1 14  ASN n 
1 15  THR n 
1 16  ASP n 
1 17  ILE n 
1 18  GLY n 
1 19  ASP n 
1 20  PRO n 
1 21  SER n 
1 22  TYR n 
1 23  PRO n 
1 24  HIS n 
1 25  ILE n 
1 26  GLY n 
1 27  ILE n 
1 28  ASP n 
1 29  ILE n 
1 30  LYS n 
1 31  SER n 
1 32  VAL n 
1 33  ARG n 
1 34  SER n 
1 35  LYS n 
1 36  LYS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TRP n 
1 41  ASN n 
1 42  MET n 
1 43  GLN n 
1 44  ASN n 
1 45  GLY n 
1 46  LYS n 
1 47  VAL n 
1 48  GLY n 
1 49  THR n 
1 50  ALA n 
1 51  HIS n 
1 52  ILE n 
1 53  ILE n 
1 54  TYR n 
1 55  ASN n 
1 56  SER n 
1 57  VAL n 
1 58  ASP n 
1 59  LYS n 
1 60  ARG n 
1 61  LEU n 
1 62  SER n 
1 63  ALA n 
1 64  VAL n 
1 65  VAL n 
1 66  SER n 
1 67  TYR n 
1 68  PRO n 
1 69  ASN n 
1 70  ALA n 
1 71  ASP n 
1 72  SER n 
1 73  ALA n 
1 74  THR n 
1 75  VAL n 
1 76  SER n 
1 77  TYR n 
1 78  ASP n 
1 79  VAL n 
1 80  ASP n 
1 81  LEU n 
1 82  ASP n 
1 83  ASN n 
1 84  VAL n 
1 85  LEU n 
1 86  PRO n 
1 87  GLU n 
1 88  TRP n 
1 89  VAL n 
1 90  ARG n 
1 91  VAL n 
1 92  GLY n 
1 93  LEU n 
1 94  SER n 
1 95  ALA n 
1 96  SER n 
1 97  THR n 
1 98  GLY n 
1 99  LEU n 
1 100 TYR n 
1 101 LYS n 
1 102 GLU n 
1 103 THR n 
1 104 ASN n 
1 105 THR n 
1 106 ILE n 
1 107 LEU n 
1 108 SER n 
1 109 TRP n 
1 110 SER n 
1 111 PHE n 
1 112 THR n 
1 113 SER n 
1 114 LYS n 
1 115 LEU n 
1 116 LYS n 
1 117 SER n 
1 118 ASN n 
1 119 SER n 
1 120 THR n 
1 121 HIS n 
1 122 GLU n 
1 123 THR n 
1 124 ASN n 
1 125 ALA n 
1 126 LEU n 
1 127 HIS n 
1 128 PHE n 
1 129 MET n 
1 130 PHE n 
1 131 ASN n 
1 132 GLN n 
1 133 PHE n 
1 134 SER n 
1 135 LYS n 
1 136 ASP n 
1 137 GLN n 
1 138 LYS n 
1 139 ASP n 
1 140 LEU n 
1 141 ILE n 
1 142 LEU n 
1 143 GLN n 
1 144 GLY n 
1 145 ASP n 
1 146 ALA n 
1 147 THR n 
1 148 THR n 
1 149 GLY n 
1 150 THR n 
1 151 ASP n 
1 152 GLY n 
1 153 ASN n 
1 154 LEU n 
1 155 GLU n 
1 156 LEU n 
1 157 THR n 
1 158 ARG n 
1 159 VAL n 
1 160 SER n 
1 161 SER n 
1 162 ASN n 
1 163 GLY n 
1 164 SER n 
1 165 PRO n 
1 166 GLN n 
1 167 GLY n 
1 168 SER n 
1 169 SER n 
1 170 VAL n 
1 171 GLY n 
1 172 ARG n 
1 173 ALA n 
1 174 LEU n 
1 175 PHE n 
1 176 TYR n 
1 177 ALA n 
1 178 PRO n 
1 179 VAL n 
1 180 HIS n 
1 181 ILE n 
1 182 TRP n 
1 183 GLU n 
1 184 SER n 
1 185 SER n 
1 186 ALA n 
1 187 VAL n 
1 188 VAL n 
1 189 ALA n 
1 190 SER n 
1 191 PHE n 
1 192 GLU n 
1 193 ALA n 
1 194 THR n 
1 195 PHE n 
1 196 THR n 
1 197 PHE n 
1 198 LEU n 
1 199 ILE n 
1 200 LYS n 
1 201 SER n 
1 202 PRO n 
1 203 ASP n 
1 204 SER n 
1 205 HIS n 
1 206 PRO n 
1 207 ALA n 
1 208 ASP n 
1 209 GLY n 
1 210 ILE n 
1 211 ALA n 
1 212 PHE n 
1 213 PHE n 
1 214 ILE n 
1 215 SER n 
1 216 ASN n 
1 217 ILE n 
1 218 ASP n 
1 219 SER n 
1 220 SER n 
1 221 ILE n 
1 222 PRO n 
1 223 SER n 
1 224 GLY n 
1 225 SER n 
1 226 THR n 
1 227 GLY n 
1 228 ARG n 
1 229 LEU n 
1 230 LEU n 
1 231 GLY n 
1 232 LEU n 
1 233 PHE n 
1 234 PRO n 
1 235 ASP n 
1 236 ALA n 
1 237 ASN n 
# 
loop_
_entity_src_nat.entity_id 
_entity_src_nat.pdbx_src_id 
_entity_src_nat.pdbx_alt_source_flag 
_entity_src_nat.pdbx_beg_seq_num 
_entity_src_nat.pdbx_end_seq_num 
_entity_src_nat.common_name 
_entity_src_nat.pdbx_organism_scientific 
_entity_src_nat.pdbx_ncbi_taxonomy_id 
_entity_src_nat.genus 
_entity_src_nat.species 
_entity_src_nat.strain 
_entity_src_nat.tissue 
_entity_src_nat.tissue_fraction 
_entity_src_nat.pdbx_secretion 
_entity_src_nat.pdbx_fragment 
_entity_src_nat.pdbx_variant 
_entity_src_nat.pdbx_cell_line 
_entity_src_nat.pdbx_atcc 
_entity_src_nat.pdbx_cellular_location 
_entity_src_nat.pdbx_organ 
_entity_src_nat.pdbx_organelle 
_entity_src_nat.pdbx_cell 
_entity_src_nat.pdbx_plasmid_name 
_entity_src_nat.pdbx_plasmid_details 
_entity_src_nat.details 
1 1 sample 1   118 'jack bean' 'Canavalia ensiformis' 3823 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 119 237 'jack bean' 'Canavalia ensiformis' 3823 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1EAT non-polymer         . 
;~{N}-[2-[(2~{S},3~{S},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxyethyl]-4-[3-[4-[2-[(2~{S},3~{S},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxyethylcarbamoyl]phenyl]imidazol-3-ium-1-yl]benzamide
;
? 'C33 H43 N4 O14 1' 719.713 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'       89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'   175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'      132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'       133.103 
CA    non-polymer         . 'CALCIUM ION' ? 'Ca 2'             40.078  
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'     146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'       147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'       75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'   156.162 
HOH   non-polymer         . WATER ? 'H2 O'             18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'      131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'      131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'   147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'    149.211 
MN    non-polymer         . 'MANGANESE (II) ION' ? 'Mn 2'             54.938  
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'      165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'       115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'       105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'       119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'    204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'      181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   1   1   ALA ALA A . n 
A 1 2   ASP 2   2   2   ASP ASP A . n 
A 1 3   THR 3   3   3   THR THR A . n 
A 1 4   ILE 4   4   4   ILE ILE A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   ALA 6   6   6   ALA ALA A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   GLU 8   8   8   GLU GLU A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  THR 11  11  11  THR THR A . n 
A 1 12  TYR 12  12  12  TYR TYR A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  ASN 14  14  14  ASN ASN A . n 
A 1 15  THR 15  15  15  THR THR A . n 
A 1 16  ASP 16  16  16  ASP ASP A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  GLY 18  18  18  GLY GLY A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  TYR 22  22  22  TYR TYR A . n 
A 1 23  PRO 23  23  23  PRO PRO A . n 
A 1 24  HIS 24  24  24  HIS HIS A . n 
A 1 25  ILE 25  25  25  ILE ILE A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  ILE 27  27  27  ILE ILE A . n 
A 1 28  ASP 28  28  28  ASP ASP A . n 
A 1 29  ILE 29  29  29  ILE ILE A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  SER 31  31  31  SER SER A . n 
A 1 32  VAL 32  32  32  VAL VAL A . n 
A 1 33  ARG 33  33  33  ARG ARG A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  LYS 35  35  35  LYS LYS A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TRP 40  40  40  TRP TRP A . n 
A 1 41  ASN 41  41  41  ASN ASN A . n 
A 1 42  MET 42  42  42  MET MET A . n 
A 1 43  GLN 43  43  43  GLN GLN A . n 
A 1 44  ASN 44  44  44  ASN ASN A . n 
A 1 45  GLY 45  45  45  GLY GLY A . n 
A 1 46  LYS 46  46  46  LYS LYS A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  THR 49  49  49  THR THR A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  HIS 51  51  51  HIS HIS A . n 
A 1 52  ILE 52  52  52  ILE ILE A . n 
A 1 53  ILE 53  53  53  ILE ILE A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  ASN 55  55  55  ASN ASN A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  VAL 57  57  57  VAL VAL A . n 
A 1 58  ASP 58  58  58  ASP ASP A . n 
A 1 59  LYS 59  59  59  LYS LYS A . n 
A 1 60  ARG 60  60  60  ARG ARG A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  VAL 64  64  64  VAL VAL A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  SER 66  66  66  SER SER A . n 
A 1 67  TYR 67  67  67  TYR TYR A . n 
A 1 68  PRO 68  68  68  PRO PRO A . n 
A 1 69  ASN 69  69  69  ASN ASN A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  ALA 73  73  73  ALA ALA A . n 
A 1 74  THR 74  74  74  THR THR A . n 
A 1 75  VAL 75  75  75  VAL VAL A . n 
A 1 76  SER 76  76  76  SER SER A . n 
A 1 77  TYR 77  77  77  TYR TYR A . n 
A 1 78  ASP 78  78  78  ASP ASP A . n 
A 1 79  VAL 79  79  79  VAL VAL A . n 
A 1 80  ASP 80  80  80  ASP ASP A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  ASP 82  82  82  ASP ASP A . n 
A 1 83  ASN 83  83  83  ASN ASN A . n 
A 1 84  VAL 84  84  84  VAL VAL A . n 
A 1 85  LEU 85  85  85  LEU LEU A . n 
A 1 86  PRO 86  86  86  PRO PRO A . n 
A 1 87  GLU 87  87  87  GLU GLU A . n 
A 1 88  TRP 88  88  88  TRP TRP A . n 
A 1 89  VAL 89  89  89  VAL VAL A . n 
A 1 90  ARG 90  90  90  ARG ARG A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  GLY 92  92  92  GLY GLY A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  SER 94  94  94  SER SER A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  SER 96  96  96  SER SER A . n 
A 1 97  THR 97  97  97  THR THR A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 TYR 100 100 100 TYR TYR A . n 
A 1 101 LYS 101 101 101 LYS LYS A . n 
A 1 102 GLU 102 102 102 GLU GLU A . n 
A 1 103 THR 103 103 103 THR THR A . n 
A 1 104 ASN 104 104 104 ASN ASN A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 LEU 107 107 107 LEU LEU A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 TRP 109 109 109 TRP TRP A . n 
A 1 110 SER 110 110 110 SER SER A . n 
A 1 111 PHE 111 111 111 PHE PHE A . n 
A 1 112 THR 112 112 112 THR THR A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 LYS 114 114 114 LYS LYS A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 LYS 116 116 116 LYS LYS A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 ASN 118 118 118 ASN ASN A . n 
A 1 119 SER 119 119 119 SER SER A . n 
A 1 120 THR 120 120 120 THR THR A . n 
A 1 121 HIS 121 121 121 HIS HIS A . n 
A 1 122 GLU 122 122 122 GLU GLU A . n 
A 1 123 THR 123 123 123 THR THR A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 HIS 127 127 127 HIS HIS A . n 
A 1 128 PHE 128 128 128 PHE PHE A . n 
A 1 129 MET 129 129 129 MET MET A . n 
A 1 130 PHE 130 130 130 PHE PHE A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 GLN 132 132 132 GLN GLN A . n 
A 1 133 PHE 133 133 133 PHE PHE A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 LYS 135 135 135 LYS LYS A . n 
A 1 136 ASP 136 136 136 ASP ASP A . n 
A 1 137 GLN 137 137 137 GLN GLN A . n 
A 1 138 LYS 138 138 138 LYS LYS A . n 
A 1 139 ASP 139 139 139 ASP ASP A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ILE 141 141 141 ILE ILE A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 GLN 143 143 143 GLN GLN A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 ALA 146 146 146 ALA ALA A . n 
A 1 147 THR 147 147 147 THR THR A . n 
A 1 148 THR 148 148 148 THR THR A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 THR 150 150 150 THR THR A . n 
A 1 151 ASP 151 151 151 ASP ASP A . n 
A 1 152 GLY 152 152 152 GLY GLY A . n 
A 1 153 ASN 153 153 153 ASN ASN A . n 
A 1 154 LEU 154 154 154 LEU LEU A . n 
A 1 155 GLU 155 155 155 GLU GLU A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 THR 157 157 157 THR THR A . n 
A 1 158 ARG 158 158 158 ARG ARG A . n 
A 1 159 VAL 159 159 159 VAL VAL A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 SER 161 161 161 SER SER A . n 
A 1 162 ASN 162 162 162 ASN ASN A . n 
A 1 163 GLY 163 163 163 GLY GLY A . n 
A 1 164 SER 164 164 164 SER SER A . n 
A 1 165 PRO 165 165 165 PRO PRO A . n 
A 1 166 GLN 166 166 166 GLN GLN A . n 
A 1 167 GLY 167 167 167 GLY GLY A . n 
A 1 168 SER 168 168 168 SER SER A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 VAL 170 170 170 VAL VAL A . n 
A 1 171 GLY 171 171 171 GLY GLY A . n 
A 1 172 ARG 172 172 172 ARG ARG A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 PHE 175 175 175 PHE PHE A . n 
A 1 176 TYR 176 176 176 TYR TYR A . n 
A 1 177 ALA 177 177 177 ALA ALA A . n 
A 1 178 PRO 178 178 178 PRO PRO A . n 
A 1 179 VAL 179 179 179 VAL VAL A . n 
A 1 180 HIS 180 180 180 HIS HIS A . n 
A 1 181 ILE 181 181 181 ILE ILE A . n 
A 1 182 TRP 182 182 182 TRP TRP A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 SER 184 184 184 SER SER A . n 
A 1 185 SER 185 185 185 SER SER A . n 
A 1 186 ALA 186 186 186 ALA ALA A . n 
A 1 187 VAL 187 187 187 VAL VAL A . n 
A 1 188 VAL 188 188 188 VAL VAL A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 SER 190 190 190 SER SER A . n 
A 1 191 PHE 191 191 191 PHE PHE A . n 
A 1 192 GLU 192 192 192 GLU GLU A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 THR 194 194 194 THR THR A . n 
A 1 195 PHE 195 195 195 PHE PHE A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 PHE 197 197 197 PHE PHE A . n 
A 1 198 LEU 198 198 198 LEU LEU A . n 
A 1 199 ILE 199 199 199 ILE ILE A . n 
A 1 200 LYS 200 200 200 LYS LYS A . n 
A 1 201 SER 201 201 201 SER SER A . n 
A 1 202 PRO 202 202 202 PRO PRO A . n 
A 1 203 ASP 203 203 203 ASP ASP A . n 
A 1 204 SER 204 204 204 SER SER A . n 
A 1 205 HIS 205 205 205 HIS HIS A . n 
A 1 206 PRO 206 206 206 PRO PRO A . n 
A 1 207 ALA 207 207 207 ALA ALA A . n 
A 1 208 ASP 208 208 208 ASP ASP A . n 
A 1 209 GLY 209 209 209 GLY GLY A . n 
A 1 210 ILE 210 210 210 ILE ILE A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 PHE 212 212 212 PHE PHE A . n 
A 1 213 PHE 213 213 213 PHE PHE A . n 
A 1 214 ILE 214 214 214 ILE ILE A . n 
A 1 215 SER 215 215 215 SER SER A . n 
A 1 216 ASN 216 216 216 ASN ASN A . n 
A 1 217 ILE 217 217 217 ILE ILE A . n 
A 1 218 ASP 218 218 218 ASP ASP A . n 
A 1 219 SER 219 219 219 SER SER A . n 
A 1 220 SER 220 220 220 SER SER A . n 
A 1 221 ILE 221 221 221 ILE ILE A . n 
A 1 222 PRO 222 222 222 PRO PRO A . n 
A 1 223 SER 223 223 223 SER SER A . n 
A 1 224 GLY 224 224 224 GLY GLY A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 GLY 227 227 227 GLY GLY A . n 
A 1 228 ARG 228 228 228 ARG ARG A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 GLY 231 231 231 GLY GLY A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 PHE 233 233 233 PHE PHE A . n 
A 1 234 PRO 234 234 234 PRO PRO A . n 
A 1 235 ASP 235 235 235 ASP ASP A . n 
A 1 236 ALA 236 236 236 ALA ALA A . n 
A 1 237 ASN 237 237 237 ASN ASN A . n 
B 1 1   ALA 1   1   1   ALA ALA B . n 
B 1 2   ASP 2   2   2   ASP ASP B . n 
B 1 3   THR 3   3   3   THR THR B . n 
B 1 4   ILE 4   4   4   ILE ILE B . n 
B 1 5   VAL 5   5   5   VAL VAL B . n 
B 1 6   ALA 6   6   6   ALA ALA B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   GLU 8   8   8   GLU GLU B . n 
B 1 9   LEU 9   9   9   LEU LEU B . n 
B 1 10  ASP 10  10  10  ASP ASP B . n 
B 1 11  THR 11  11  11  THR THR B . n 
B 1 12  TYR 12  12  12  TYR TYR B . n 
B 1 13  PRO 13  13  13  PRO PRO B . n 
B 1 14  ASN 14  14  14  ASN ASN B . n 
B 1 15  THR 15  15  15  THR THR B . n 
B 1 16  ASP 16  16  16  ASP ASP B . n 
B 1 17  ILE 17  17  17  ILE ILE B . n 
B 1 18  GLY 18  18  18  GLY GLY B . n 
B 1 19  ASP 19  19  19  ASP ASP B . n 
B 1 20  PRO 20  20  20  PRO PRO B . n 
B 1 21  SER 21  21  21  SER SER B . n 
B 1 22  TYR 22  22  22  TYR TYR B . n 
B 1 23  PRO 23  23  23  PRO PRO B . n 
B 1 24  HIS 24  24  24  HIS HIS B . n 
B 1 25  ILE 25  25  25  ILE ILE B . n 
B 1 26  GLY 26  26  26  GLY GLY B . n 
B 1 27  ILE 27  27  27  ILE ILE B . n 
B 1 28  ASP 28  28  28  ASP ASP B . n 
B 1 29  ILE 29  29  29  ILE ILE B . n 
B 1 30  LYS 30  30  30  LYS LYS B . n 
B 1 31  SER 31  31  31  SER SER B . n 
B 1 32  VAL 32  32  32  VAL VAL B . n 
B 1 33  ARG 33  33  33  ARG ARG B . n 
B 1 34  SER 34  34  34  SER SER B . n 
B 1 35  LYS 35  35  35  LYS LYS B . n 
B 1 36  LYS 36  36  36  LYS LYS B . n 
B 1 37  THR 37  37  37  THR THR B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  LYS 39  39  39  LYS LYS B . n 
B 1 40  TRP 40  40  40  TRP TRP B . n 
B 1 41  ASN 41  41  41  ASN ASN B . n 
B 1 42  MET 42  42  42  MET MET B . n 
B 1 43  GLN 43  43  43  GLN GLN B . n 
B 1 44  ASN 44  44  44  ASN ASN B . n 
B 1 45  GLY 45  45  45  GLY GLY B . n 
B 1 46  LYS 46  46  46  LYS LYS B . n 
B 1 47  VAL 47  47  47  VAL VAL B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  THR 49  49  49  THR THR B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  HIS 51  51  51  HIS HIS B . n 
B 1 52  ILE 52  52  52  ILE ILE B . n 
B 1 53  ILE 53  53  53  ILE ILE B . n 
B 1 54  TYR 54  54  54  TYR TYR B . n 
B 1 55  ASN 55  55  55  ASN ASN B . n 
B 1 56  SER 56  56  56  SER SER B . n 
B 1 57  VAL 57  57  57  VAL VAL B . n 
B 1 58  ASP 58  58  58  ASP ASP B . n 
B 1 59  LYS 59  59  59  LYS LYS B . n 
B 1 60  ARG 60  60  60  ARG ARG B . n 
B 1 61  LEU 61  61  61  LEU LEU B . n 
B 1 62  SER 62  62  62  SER SER B . n 
B 1 63  ALA 63  63  63  ALA ALA B . n 
B 1 64  VAL 64  64  64  VAL VAL B . n 
B 1 65  VAL 65  65  65  VAL VAL B . n 
B 1 66  SER 66  66  66  SER SER B . n 
B 1 67  TYR 67  67  67  TYR TYR B . n 
B 1 68  PRO 68  68  68  PRO PRO B . n 
B 1 69  ASN 69  69  69  ASN ASN B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  ASP 71  71  71  ASP ASP B . n 
B 1 72  SER 72  72  72  SER SER B . n 
B 1 73  ALA 73  73  73  ALA ALA B . n 
B 1 74  THR 74  74  74  THR THR B . n 
B 1 75  VAL 75  75  75  VAL VAL B . n 
B 1 76  SER 76  76  76  SER SER B . n 
B 1 77  TYR 77  77  77  TYR TYR B . n 
B 1 78  ASP 78  78  78  ASP ASP B . n 
B 1 79  VAL 79  79  79  VAL VAL B . n 
B 1 80  ASP 80  80  80  ASP ASP B . n 
B 1 81  LEU 81  81  81  LEU LEU B . n 
B 1 82  ASP 82  82  82  ASP ASP B . n 
B 1 83  ASN 83  83  83  ASN ASN B . n 
B 1 84  VAL 84  84  84  VAL VAL B . n 
B 1 85  LEU 85  85  85  LEU LEU B . n 
B 1 86  PRO 86  86  86  PRO PRO B . n 
B 1 87  GLU 87  87  87  GLU GLU B . n 
B 1 88  TRP 88  88  88  TRP TRP B . n 
B 1 89  VAL 89  89  89  VAL VAL B . n 
B 1 90  ARG 90  90  90  ARG ARG B . n 
B 1 91  VAL 91  91  91  VAL VAL B . n 
B 1 92  GLY 92  92  92  GLY GLY B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  SER 94  94  94  SER SER B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  SER 96  96  96  SER SER B . n 
B 1 97  THR 97  97  97  THR THR B . n 
B 1 98  GLY 98  98  98  GLY GLY B . n 
B 1 99  LEU 99  99  99  LEU LEU B . n 
B 1 100 TYR 100 100 100 TYR TYR B . n 
B 1 101 LYS 101 101 101 LYS LYS B . n 
B 1 102 GLU 102 102 102 GLU GLU B . n 
B 1 103 THR 103 103 103 THR THR B . n 
B 1 104 ASN 104 104 104 ASN ASN B . n 
B 1 105 THR 105 105 105 THR THR B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 LEU 107 107 107 LEU LEU B . n 
B 1 108 SER 108 108 108 SER SER B . n 
B 1 109 TRP 109 109 109 TRP TRP B . n 
B 1 110 SER 110 110 110 SER SER B . n 
B 1 111 PHE 111 111 111 PHE PHE B . n 
B 1 112 THR 112 112 112 THR THR B . n 
B 1 113 SER 113 113 113 SER SER B . n 
B 1 114 LYS 114 114 114 LYS LYS B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 LYS 116 116 116 LYS LYS B . n 
B 1 117 SER 117 117 117 SER SER B . n 
B 1 118 ASN 118 118 118 ASN ASN B . n 
B 1 119 SER 119 119 119 SER SER B . n 
B 1 120 THR 120 120 120 THR THR B . n 
B 1 121 HIS 121 121 121 HIS HIS B . n 
B 1 122 GLU 122 122 122 GLU GLU B . n 
B 1 123 THR 123 123 123 THR THR B . n 
B 1 124 ASN 124 124 124 ASN ASN B . n 
B 1 125 ALA 125 125 125 ALA ALA B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 HIS 127 127 127 HIS HIS B . n 
B 1 128 PHE 128 128 128 PHE PHE B . n 
B 1 129 MET 129 129 129 MET MET B . n 
B 1 130 PHE 130 130 130 PHE PHE B . n 
B 1 131 ASN 131 131 131 ASN ASN B . n 
B 1 132 GLN 132 132 132 GLN GLN B . n 
B 1 133 PHE 133 133 133 PHE PHE B . n 
B 1 134 SER 134 134 134 SER SER B . n 
B 1 135 LYS 135 135 135 LYS LYS B . n 
B 1 136 ASP 136 136 136 ASP ASP B . n 
B 1 137 GLN 137 137 137 GLN GLN B . n 
B 1 138 LYS 138 138 138 LYS LYS B . n 
B 1 139 ASP 139 139 139 ASP ASP B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ILE 141 141 141 ILE ILE B . n 
B 1 142 LEU 142 142 142 LEU LEU B . n 
B 1 143 GLN 143 143 143 GLN GLN B . n 
B 1 144 GLY 144 144 144 GLY GLY B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 ALA 146 146 146 ALA ALA B . n 
B 1 147 THR 147 147 147 THR THR B . n 
B 1 148 THR 148 148 148 THR THR B . n 
B 1 149 GLY 149 149 149 GLY GLY B . n 
B 1 150 THR 150 150 150 THR THR B . n 
B 1 151 ASP 151 151 151 ASP ASP B . n 
B 1 152 GLY 152 152 152 GLY GLY B . n 
B 1 153 ASN 153 153 153 ASN ASN B . n 
B 1 154 LEU 154 154 154 LEU LEU B . n 
B 1 155 GLU 155 155 155 GLU GLU B . n 
B 1 156 LEU 156 156 156 LEU LEU B . n 
B 1 157 THR 157 157 157 THR THR B . n 
B 1 158 ARG 158 158 158 ARG ARG B . n 
B 1 159 VAL 159 159 159 VAL VAL B . n 
B 1 160 SER 160 160 160 SER SER B . n 
B 1 161 SER 161 161 161 SER SER B . n 
B 1 162 ASN 162 162 162 ASN ASN B . n 
B 1 163 GLY 163 163 163 GLY GLY B . n 
B 1 164 SER 164 164 164 SER SER B . n 
B 1 165 PRO 165 165 165 PRO PRO B . n 
B 1 166 GLN 166 166 166 GLN GLN B . n 
B 1 167 GLY 167 167 167 GLY GLY B . n 
B 1 168 SER 168 168 168 SER SER B . n 
B 1 169 SER 169 169 169 SER SER B . n 
B 1 170 VAL 170 170 170 VAL VAL B . n 
B 1 171 GLY 171 171 171 GLY GLY B . n 
B 1 172 ARG 172 172 172 ARG ARG B . n 
B 1 173 ALA 173 173 173 ALA ALA B . n 
B 1 174 LEU 174 174 174 LEU LEU B . n 
B 1 175 PHE 175 175 175 PHE PHE B . n 
B 1 176 TYR 176 176 176 TYR TYR B . n 
B 1 177 ALA 177 177 177 ALA ALA B . n 
B 1 178 PRO 178 178 178 PRO PRO B . n 
B 1 179 VAL 179 179 179 VAL VAL B . n 
B 1 180 HIS 180 180 180 HIS HIS B . n 
B 1 181 ILE 181 181 181 ILE ILE B . n 
B 1 182 TRP 182 182 182 TRP TRP B . n 
B 1 183 GLU 183 183 183 GLU GLU B . n 
B 1 184 SER 184 184 184 SER SER B . n 
B 1 185 SER 185 185 185 SER SER B . n 
B 1 186 ALA 186 186 186 ALA ALA B . n 
B 1 187 VAL 187 187 187 VAL VAL B . n 
B 1 188 VAL 188 188 188 VAL VAL B . n 
B 1 189 ALA 189 189 189 ALA ALA B . n 
B 1 190 SER 190 190 190 SER SER B . n 
B 1 191 PHE 191 191 191 PHE PHE B . n 
B 1 192 GLU 192 192 192 GLU GLU B . n 
B 1 193 ALA 193 193 193 ALA ALA B . n 
B 1 194 THR 194 194 194 THR THR B . n 
B 1 195 PHE 195 195 195 PHE PHE B . n 
B 1 196 THR 196 196 196 THR THR B . n 
B 1 197 PHE 197 197 197 PHE PHE B . n 
B 1 198 LEU 198 198 198 LEU LEU B . n 
B 1 199 ILE 199 199 199 ILE ILE B . n 
B 1 200 LYS 200 200 200 LYS LYS B . n 
B 1 201 SER 201 201 201 SER SER B . n 
B 1 202 PRO 202 202 202 PRO PRO B . n 
B 1 203 ASP 203 203 203 ASP ASP B . n 
B 1 204 SER 204 204 204 SER SER B . n 
B 1 205 HIS 205 205 205 HIS HIS B . n 
B 1 206 PRO 206 206 206 PRO PRO B . n 
B 1 207 ALA 207 207 207 ALA ALA B . n 
B 1 208 ASP 208 208 208 ASP ASP B . n 
B 1 209 GLY 209 209 209 GLY GLY B . n 
B 1 210 ILE 210 210 210 ILE ILE B . n 
B 1 211 ALA 211 211 211 ALA ALA B . n 
B 1 212 PHE 212 212 212 PHE PHE B . n 
B 1 213 PHE 213 213 213 PHE PHE B . n 
B 1 214 ILE 214 214 214 ILE ILE B . n 
B 1 215 SER 215 215 215 SER SER B . n 
B 1 216 ASN 216 216 216 ASN ASN B . n 
B 1 217 ILE 217 217 217 ILE ILE B . n 
B 1 218 ASP 218 218 218 ASP ASP B . n 
B 1 219 SER 219 219 219 SER SER B . n 
B 1 220 SER 220 220 220 SER SER B . n 
B 1 221 ILE 221 221 221 ILE ILE B . n 
B 1 222 PRO 222 222 222 PRO PRO B . n 
B 1 223 SER 223 223 223 SER SER B . n 
B 1 224 GLY 224 224 224 GLY GLY B . n 
B 1 225 SER 225 225 225 SER SER B . n 
B 1 226 THR 226 226 226 THR THR B . n 
B 1 227 GLY 227 227 227 GLY GLY B . n 
B 1 228 ARG 228 228 228 ARG ARG B . n 
B 1 229 LEU 229 229 229 LEU LEU B . n 
B 1 230 LEU 230 230 230 LEU LEU B . n 
B 1 231 GLY 231 231 231 GLY GLY B . n 
B 1 232 LEU 232 232 232 LEU LEU B . n 
B 1 233 PHE 233 233 233 PHE PHE B . n 
B 1 234 PRO 234 234 234 PRO PRO B . n 
B 1 235 ASP 235 235 235 ASP ASP B . n 
B 1 236 ALA 236 236 236 ALA ALA B . n 
B 1 237 ASN 237 237 237 ASN ASN B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1EAT 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1EAT 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 MN    1 301 1   MN    MN  A . 
D 3 CA    1 302 1   CA    CA  A . 
E 4 A1EAT 1 301 301 A1EAT M2I B . 
F 2 MN    1 302 2   MN    MN  B . 
G 3 CA    1 303 2   CA    CA  B . 
H 5 HOH   1 401 12  HOH   HOH A . 
H 5 HOH   2 402 11  HOH   HOH A . 
H 5 HOH   3 403 8   HOH   HOH A . 
H 5 HOH   4 404 4   HOH   HOH A . 
H 5 HOH   5 405 6   HOH   HOH A . 
H 5 HOH   6 406 7   HOH   HOH A . 
H 5 HOH   7 407 1   HOH   HOH A . 
H 5 HOH   8 408 15  HOH   HOH A . 
H 5 HOH   9 409 13  HOH   HOH A . 
I 5 HOH   1 401 10  HOH   HOH B . 
I 5 HOH   2 402 14  HOH   HOH B . 
I 5 HOH   3 403 3   HOH   HOH B . 
I 5 HOH   4 404 2   HOH   HOH B . 
I 5 HOH   5 405 5   HOH   HOH B . 
I 5 HOH   6 406 9   HOH   HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0238 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2    ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   127.27 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9J1B 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     117.380 
_cell.length_a_esd                 ? 
_cell.length_b                     113.720 
_cell.length_b_esd                 ? 
_cell.length_c                     83.710 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9J1B 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9J1B 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             4.34 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          71.65 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'buffer: 20 mM HEPES, 5 mM CaCl2, 5 mM MnCl2; pH = 7.2, precipitant: Ammonium phosphate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-06-08 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9J1B 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.48 
_reflns.d_resolution_low                               28.76 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     30883 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          18.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.93 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.068 
_reflns.pdbx_Rpim_I_all                                0.027 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.062 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.48 
_reflns_shell.d_res_low                                     2.54 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           9200 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2220 
_reflns_shell.percent_possible_obs                          96.9 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               4.1 
_reflns_shell.pdbx_chi_squared                              0.70 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     3.1 
_reflns_shell.pdbx_Rrim_I_all                               0.631 
_reflns_shell.pdbx_Rpim_I_all                               0.306 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.636 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.547 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.02 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.02 
_refine.aniso_B[2][2]                            0.08 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.03 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               52.585 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.954 
_refine.correlation_coeff_Fo_to_Fc_free          0.933 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9J1B 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.48 
_refine.ls_d_res_low                             28.76 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     28944 
_refine.ls_number_reflns_R_free                  1472 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.03 
_refine.ls_percent_reflns_R_free                 4.8 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18949 
_refine.ls_R_factor_R_free                       0.22756 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.18754 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      4P9W 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.243 
_refine.pdbx_overall_ESU_R_Free                  0.206 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             7.094 
_refine.overall_SU_ML                            0.158 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.48 
_refine_hist.d_res_low                        28.76 
_refine_hist.number_atoms_solvent             15 
_refine_hist.number_atoms_total               3688 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3618 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         55 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.010  0.013  3757 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  3343 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.851  1.653  5125 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.252  1.590  7792 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 9.577  5.000  472  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 37.910 23.810 168  ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.634 15.000 578  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 14.531 15.000 12   ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.067  0.200  520  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  4221 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  763  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 5.098  5.550  1894 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 5.097  5.549  1893 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 7.522  8.318  2365 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 7.520  8.317  2366 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.531  5.933  1862 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 5.529  5.932  1863 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 8.039  8.713  2761 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 10.468 62.466 3782 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 10.467 62.469 3780 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.480 
_refine_ls_shell.d_res_low                        2.544 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             96 
_refine_ls_shell.number_reflns_R_work             2081 
_refine_ls_shell.percent_reflns_obs               95.02 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.268 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.336 
# 
_struct.entry_id                     9J1B 
_struct.title                        'Structure of ConA/IMI-Man' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9J1B 
_struct_keywords.text            'Complex, Lectin, Ligand, SUGAR BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'SUGAR BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 2 ? 
G N N 3 ? 
H N N 5 ? 
I N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP CONA_CANEN P02866 ? 1 
;ADTIVAVELDTYPNTDIGDPSYPHIGIDIKSVRSKKTAKWNMQNGKVGTAHIIYNSVDKRLSAVVSYPNADSATVSYDVD
LDNVLPEWVRVGLSASTGLYKETNTILSWSFTSKLKSN
;
164 
2 UNP CONA_CANEN P02866 ? 1 
;STHETNALHFMFNQFSKDQKDLILQGDATTGTDGNLELTRVSSNGSPQGSSVGRALFYAPVHIWESSAVVASFEATFTFL
IKSPDSHPADGIAFFISNIDSSIPSGSTGRLLGLFPDAN
;
30  
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9J1B A 1   ? 118 ? P02866 164 ? 281 ? 1   118 
2 2 9J1B A 119 ? 237 ? P02866 30  ? 148 ? 119 237 
3 1 9J1B B 1   ? 118 ? P02866 164 ? 281 ? 1   118 
4 2 9J1B B 119 ? 237 ? P02866 30  ? 148 ? 119 237 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 9380  ? 
1 MORE         -106  ? 
1 'SSA (A^2)'  35270 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000   0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 2_556 -x,y,-z+1 -1.0000000000 0.0000000000 0.0000000000 -50.6924160708 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 66.6156366997 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ASN A 14  ? GLY A 18  ? ASN A 14  GLY A 18  5 ? 5 
HELX_P HELX_P2 AA2 ASP A 80  ? VAL A 84  ? ASP A 80  VAL A 84  5 ? 5 
HELX_P HELX_P3 AA3 THR A 226 ? LEU A 230 ? THR A 226 LEU A 230 5 ? 5 
HELX_P HELX_P4 AA4 ASN B 14  ? GLY B 18  ? ASN B 14  GLY B 18  5 ? 5 
HELX_P HELX_P5 AA5 THR B 226 ? LEU B 230 ? THR B 226 LEU B 230 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A GLU 8  OE2 ? ? ? 1_555 C MN  . MN ? ? A GLU 8   A MN  301 1_555 ? ? ? ? ? ? ? 2.196 ? ? 
metalc2  metalc ? ? A ASP 10 OD2 ? ? ? 1_555 C MN  . MN ? ? A ASP 10  A MN  301 1_555 ? ? ? ? ? ? ? 2.136 ? ? 
metalc3  metalc ? ? A ASP 10 OD1 ? ? ? 1_555 D CA  . CA ? ? A ASP 10  A CA  302 1_555 ? ? ? ? ? ? ? 2.302 ? ? 
metalc4  metalc ? ? A ASP 10 OD2 ? ? ? 1_555 D CA  . CA ? ? A ASP 10  A CA  302 1_555 ? ? ? ? ? ? ? 2.400 ? ? 
metalc5  metalc ? ? A TYR 12 O   ? ? ? 1_555 D CA  . CA ? ? A TYR 12  A CA  302 1_555 ? ? ? ? ? ? ? 2.310 ? ? 
metalc6  metalc ? ? A ASN 14 OD1 ? ? ? 1_555 D CA  . CA ? ? A ASN 14  A CA  302 1_555 ? ? ? ? ? ? ? 2.497 ? ? 
metalc7  metalc ? ? A ASP 19 OD1 ? ? ? 1_555 C MN  . MN ? ? A ASP 19  A MN  301 1_555 ? ? ? ? ? ? ? 2.237 ? ? 
metalc8  metalc ? ? A ASP 19 OD2 ? ? ? 1_555 D CA  . CA ? ? A ASP 19  A CA  302 1_555 ? ? ? ? ? ? ? 2.315 ? ? 
metalc9  metalc ? ? A HIS 24 NE2 ? ? ? 1_555 C MN  . MN ? ? A HIS 24  A MN  301 1_555 ? ? ? ? ? ? ? 2.145 ? ? 
metalc10 metalc ? ? C MN  .  MN  ? ? ? 1_555 H HOH . O  ? ? A MN  301 A HOH 403 1_555 ? ? ? ? ? ? ? 2.127 ? ? 
metalc11 metalc ? ? C MN  .  MN  ? ? ? 1_555 H HOH . O  ? ? A MN  301 A HOH 404 1_555 ? ? ? ? ? ? ? 2.254 ? ? 
metalc12 metalc ? ? D CA  .  CA  ? ? ? 1_555 H HOH . O  ? ? A CA  302 A HOH 405 1_555 ? ? ? ? ? ? ? 2.489 ? ? 
metalc13 metalc ? ? D CA  .  CA  ? ? ? 1_555 H HOH . O  ? ? A CA  302 A HOH 407 1_555 ? ? ? ? ? ? ? 2.352 ? ? 
metalc14 metalc ? ? B GLU 8  OE2 ? ? ? 1_555 F MN  . MN ? ? B GLU 8   B MN  302 1_555 ? ? ? ? ? ? ? 2.157 ? ? 
metalc15 metalc ? ? B ASP 10 OD2 ? ? ? 1_555 F MN  . MN ? ? B ASP 10  B MN  302 1_555 ? ? ? ? ? ? ? 2.128 ? ? 
metalc16 metalc ? ? B ASP 10 OD1 ? ? ? 1_555 G CA  . CA ? ? B ASP 10  B CA  303 1_555 ? ? ? ? ? ? ? 2.642 ? ? 
metalc17 metalc ? ? B ASP 10 OD2 ? ? ? 1_555 G CA  . CA ? ? B ASP 10  B CA  303 1_555 ? ? ? ? ? ? ? 2.523 ? ? 
metalc18 metalc ? ? B TYR 12 O   ? ? ? 1_555 G CA  . CA ? ? B TYR 12  B CA  303 1_555 ? ? ? ? ? ? ? 2.367 ? ? 
metalc19 metalc ? ? B ASN 14 OD1 ? ? ? 1_555 G CA  . CA ? ? B ASN 14  B CA  303 1_555 ? ? ? ? ? ? ? 2.303 ? ? 
metalc20 metalc ? ? B ASP 19 OD1 ? ? ? 1_555 F MN  . MN ? ? B ASP 19  B MN  302 1_555 ? ? ? ? ? ? ? 2.015 ? ? 
metalc21 metalc ? ? B ASP 19 OD2 ? ? ? 1_555 G CA  . CA ? ? B ASP 19  B CA  303 1_555 ? ? ? ? ? ? ? 2.209 ? ? 
metalc22 metalc ? ? B HIS 24 NE2 ? ? ? 1_555 F MN  . MN ? ? B HIS 24  B MN  302 1_555 ? ? ? ? ? ? ? 2.283 ? ? 
metalc23 metalc ? ? F MN  .  MN  ? ? ? 1_555 I HOH . O  ? ? B MN  302 B HOH 401 1_555 ? ? ? ? ? ? ? 2.053 ? ? 
metalc24 metalc ? ? F MN  .  MN  ? ? ? 1_555 I HOH . O  ? ? B MN  302 B HOH 402 1_555 ? ? ? ? ? ? ? 2.324 ? ? 
metalc25 metalc ? ? G CA  .  CA  ? ? ? 1_555 I HOH . O  ? ? B CA  303 B HOH 404 1_555 ? ? ? ? ? ? ? 2.281 ? ? 
metalc26 metalc ? ? G CA  .  CA  ? ? ? 1_555 I HOH . O  ? ? B CA  303 B HOH 405 1_555 ? ? ? ? ? ? ? 2.236 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OE2 ? A GLU 8  ? A GLU 8   ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 OD2 ? A ASP 10 ? A ASP 10  ? 1_555 90.1  ? 
2  OE2 ? A GLU 8  ? A GLU 8   ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 OD1 ? A ASP 19 ? A ASP 19  ? 1_555 173.2 ? 
3  OD2 ? A ASP 10 ? A ASP 10  ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 OD1 ? A ASP 19 ? A ASP 19  ? 1_555 94.9  ? 
4  OE2 ? A GLU 8  ? A GLU 8   ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 NE2 ? A HIS 24 ? A HIS 24  ? 1_555 95.9  ? 
5  OD2 ? A ASP 10 ? A ASP 10  ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 NE2 ? A HIS 24 ? A HIS 24  ? 1_555 87.6  ? 
6  OD1 ? A ASP 19 ? A ASP 19  ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 NE2 ? A HIS 24 ? A HIS 24  ? 1_555 88.9  ? 
7  OE2 ? A GLU 8  ? A GLU 8   ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 O   ? H HOH .  ? A HOH 403 ? 1_555 95.7  ? 
8  OD2 ? A ASP 10 ? A ASP 10  ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 O   ? H HOH .  ? A HOH 403 ? 1_555 174.2 ? 
9  OD1 ? A ASP 19 ? A ASP 19  ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 O   ? H HOH .  ? A HOH 403 ? 1_555 79.4  ? 
10 NE2 ? A HIS 24 ? A HIS 24  ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 O   ? H HOH .  ? A HOH 403 ? 1_555 91.5  ? 
11 OE2 ? A GLU 8  ? A GLU 8   ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 O   ? H HOH .  ? A HOH 404 ? 1_555 81.2  ? 
12 OD2 ? A ASP 10 ? A ASP 10  ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 O   ? H HOH .  ? A HOH 404 ? 1_555 92.3  ? 
13 OD1 ? A ASP 19 ? A ASP 19  ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 O   ? H HOH .  ? A HOH 404 ? 1_555 93.9  ? 
14 NE2 ? A HIS 24 ? A HIS 24  ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 O   ? H HOH .  ? A HOH 404 ? 1_555 177.1 ? 
15 O   ? H HOH .  ? A HOH 403 ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 O   ? H HOH .  ? A HOH 404 ? 1_555 88.9  ? 
16 OD1 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? D CA . ? A CA 302 ? 1_555 OD2 ? A ASP 10 ? A ASP 10  ? 1_555 54.2  ? 
17 OD1 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? D CA . ? A CA 302 ? 1_555 O   ? A TYR 12 ? A TYR 12  ? 1_555 81.4  ? 
18 OD2 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? D CA . ? A CA 302 ? 1_555 O   ? A TYR 12 ? A TYR 12  ? 1_555 119.0 ? 
19 OD1 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? D CA . ? A CA 302 ? 1_555 OD1 ? A ASN 14 ? A ASN 14  ? 1_555 145.3 ? 
20 OD2 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? D CA . ? A CA 302 ? 1_555 OD1 ? A ASN 14 ? A ASN 14  ? 1_555 160.3 ? 
21 O   ? A TYR 12 ? A TYR 12  ? 1_555 CA ? D CA . ? A CA 302 ? 1_555 OD1 ? A ASN 14 ? A ASN 14  ? 1_555 75.4  ? 
22 OD1 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? D CA . ? A CA 302 ? 1_555 OD2 ? A ASP 19 ? A ASP 19  ? 1_555 115.4 ? 
23 OD2 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? D CA . ? A CA 302 ? 1_555 OD2 ? A ASP 19 ? A ASP 19  ? 1_555 81.8  ? 
24 O   ? A TYR 12 ? A TYR 12  ? 1_555 CA ? D CA . ? A CA 302 ? 1_555 OD2 ? A ASP 19 ? A ASP 19  ? 1_555 83.2  ? 
25 OD1 ? A ASN 14 ? A ASN 14  ? 1_555 CA ? D CA . ? A CA 302 ? 1_555 OD2 ? A ASP 19 ? A ASP 19  ? 1_555 87.3  ? 
26 OD1 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? D CA . ? A CA 302 ? 1_555 O   ? H HOH .  ? A HOH 405 ? 1_555 111.1 ? 
27 OD2 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? D CA . ? A CA 302 ? 1_555 O   ? H HOH .  ? A HOH 405 ? 1_555 76.0  ? 
28 O   ? A TYR 12 ? A TYR 12  ? 1_555 CA ? D CA . ? A CA 302 ? 1_555 O   ? H HOH .  ? A HOH 405 ? 1_555 164.9 ? 
29 OD1 ? A ASN 14 ? A ASN 14  ? 1_555 CA ? D CA . ? A CA 302 ? 1_555 O   ? H HOH .  ? A HOH 405 ? 1_555 89.6  ? 
30 OD2 ? A ASP 19 ? A ASP 19  ? 1_555 CA ? D CA . ? A CA 302 ? 1_555 O   ? H HOH .  ? A HOH 405 ? 1_555 98.2  ? 
31 OD1 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? D CA . ? A CA 302 ? 1_555 O   ? H HOH .  ? A HOH 407 ? 1_555 72.2  ? 
32 OD2 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? D CA . ? A CA 302 ? 1_555 O   ? H HOH .  ? A HOH 407 ? 1_555 110.2 ? 
33 O   ? A TYR 12 ? A TYR 12  ? 1_555 CA ? D CA . ? A CA 302 ? 1_555 O   ? H HOH .  ? A HOH 407 ? 1_555 88.8  ? 
34 OD1 ? A ASN 14 ? A ASN 14  ? 1_555 CA ? D CA . ? A CA 302 ? 1_555 O   ? H HOH .  ? A HOH 407 ? 1_555 81.8  ? 
35 OD2 ? A ASP 19 ? A ASP 19  ? 1_555 CA ? D CA . ? A CA 302 ? 1_555 O   ? H HOH .  ? A HOH 407 ? 1_555 167.8 ? 
36 O   ? H HOH .  ? A HOH 405 ? 1_555 CA ? D CA . ? A CA 302 ? 1_555 O   ? H HOH .  ? A HOH 407 ? 1_555 87.2  ? 
37 OE2 ? B GLU 8  ? B GLU 8   ? 1_555 MN ? F MN . ? B MN 302 ? 1_555 OD2 ? B ASP 10 ? B ASP 10  ? 1_555 94.2  ? 
38 OE2 ? B GLU 8  ? B GLU 8   ? 1_555 MN ? F MN . ? B MN 302 ? 1_555 OD1 ? B ASP 19 ? B ASP 19  ? 1_555 163.7 ? 
39 OD2 ? B ASP 10 ? B ASP 10  ? 1_555 MN ? F MN . ? B MN 302 ? 1_555 OD1 ? B ASP 19 ? B ASP 19  ? 1_555 100.2 ? 
40 OE2 ? B GLU 8  ? B GLU 8   ? 1_555 MN ? F MN . ? B MN 302 ? 1_555 NE2 ? B HIS 24 ? B HIS 24  ? 1_555 93.9  ? 
41 OD2 ? B ASP 10 ? B ASP 10  ? 1_555 MN ? F MN . ? B MN 302 ? 1_555 NE2 ? B HIS 24 ? B HIS 24  ? 1_555 86.7  ? 
42 OD1 ? B ASP 19 ? B ASP 19  ? 1_555 MN ? F MN . ? B MN 302 ? 1_555 NE2 ? B HIS 24 ? B HIS 24  ? 1_555 94.6  ? 
43 OE2 ? B GLU 8  ? B GLU 8   ? 1_555 MN ? F MN . ? B MN 302 ? 1_555 O   ? I HOH .  ? B HOH 401 ? 1_555 80.9  ? 
44 OD2 ? B ASP 10 ? B ASP 10  ? 1_555 MN ? F MN . ? B MN 302 ? 1_555 O   ? I HOH .  ? B HOH 401 ? 1_555 93.9  ? 
45 OD1 ? B ASP 19 ? B ASP 19  ? 1_555 MN ? F MN . ? B MN 302 ? 1_555 O   ? I HOH .  ? B HOH 401 ? 1_555 90.4  ? 
46 NE2 ? B HIS 24 ? B HIS 24  ? 1_555 MN ? F MN . ? B MN 302 ? 1_555 O   ? I HOH .  ? B HOH 401 ? 1_555 174.8 ? 
47 OE2 ? B GLU 8  ? B GLU 8   ? 1_555 MN ? F MN . ? B MN 302 ? 1_555 O   ? I HOH .  ? B HOH 402 ? 1_555 79.3  ? 
48 OD2 ? B ASP 10 ? B ASP 10  ? 1_555 MN ? F MN . ? B MN 302 ? 1_555 O   ? I HOH .  ? B HOH 402 ? 1_555 172.7 ? 
49 OD1 ? B ASP 19 ? B ASP 19  ? 1_555 MN ? F MN . ? B MN 302 ? 1_555 O   ? I HOH .  ? B HOH 402 ? 1_555 86.7  ? 
50 NE2 ? B HIS 24 ? B HIS 24  ? 1_555 MN ? F MN . ? B MN 302 ? 1_555 O   ? I HOH .  ? B HOH 402 ? 1_555 90.4  ? 
51 O   ? I HOH .  ? B HOH 401 ? 1_555 MN ? F MN . ? B MN 302 ? 1_555 O   ? I HOH .  ? B HOH 402 ? 1_555 88.4  ? 
52 OD1 ? B ASP 10 ? B ASP 10  ? 1_555 CA ? G CA . ? B CA 303 ? 1_555 OD2 ? B ASP 10 ? B ASP 10  ? 1_555 51.3  ? 
53 OD1 ? B ASP 10 ? B ASP 10  ? 1_555 CA ? G CA . ? B CA 303 ? 1_555 O   ? B TYR 12 ? B TYR 12  ? 1_555 77.3  ? 
54 OD2 ? B ASP 10 ? B ASP 10  ? 1_555 CA ? G CA . ? B CA 303 ? 1_555 O   ? B TYR 12 ? B TYR 12  ? 1_555 113.6 ? 
55 OD1 ? B ASP 10 ? B ASP 10  ? 1_555 CA ? G CA . ? B CA 303 ? 1_555 OD1 ? B ASN 14 ? B ASN 14  ? 1_555 147.2 ? 
56 OD2 ? B ASP 10 ? B ASP 10  ? 1_555 CA ? G CA . ? B CA 303 ? 1_555 OD1 ? B ASN 14 ? B ASN 14  ? 1_555 161.3 ? 
57 O   ? B TYR 12 ? B TYR 12  ? 1_555 CA ? G CA . ? B CA 303 ? 1_555 OD1 ? B ASN 14 ? B ASN 14  ? 1_555 80.7  ? 
58 OD1 ? B ASP 10 ? B ASP 10  ? 1_555 CA ? G CA . ? B CA 303 ? 1_555 OD2 ? B ASP 19 ? B ASP 19  ? 1_555 115.0 ? 
59 OD2 ? B ASP 10 ? B ASP 10  ? 1_555 CA ? G CA . ? B CA 303 ? 1_555 OD2 ? B ASP 19 ? B ASP 19  ? 1_555 75.9  ? 
60 O   ? B TYR 12 ? B TYR 12  ? 1_555 CA ? G CA . ? B CA 303 ? 1_555 OD2 ? B ASP 19 ? B ASP 19  ? 1_555 96.1  ? 
61 OD1 ? B ASN 14 ? B ASN 14  ? 1_555 CA ? G CA . ? B CA 303 ? 1_555 OD2 ? B ASP 19 ? B ASP 19  ? 1_555 91.3  ? 
62 OD1 ? B ASP 10 ? B ASP 10  ? 1_555 CA ? G CA . ? B CA 303 ? 1_555 O   ? I HOH .  ? B HOH 404 ? 1_555 73.1  ? 
63 OD2 ? B ASP 10 ? B ASP 10  ? 1_555 CA ? G CA . ? B CA 303 ? 1_555 O   ? I HOH .  ? B HOH 404 ? 1_555 109.1 ? 
64 O   ? B TYR 12 ? B TYR 12  ? 1_555 CA ? G CA . ? B CA 303 ? 1_555 O   ? I HOH .  ? B HOH 404 ? 1_555 88.2  ? 
65 OD1 ? B ASN 14 ? B ASN 14  ? 1_555 CA ? G CA . ? B CA 303 ? 1_555 O   ? I HOH .  ? B HOH 404 ? 1_555 82.1  ? 
66 OD2 ? B ASP 19 ? B ASP 19  ? 1_555 CA ? G CA . ? B CA 303 ? 1_555 O   ? I HOH .  ? B HOH 404 ? 1_555 171.5 ? 
67 OD1 ? B ASP 10 ? B ASP 10  ? 1_555 CA ? G CA . ? B CA 303 ? 1_555 O   ? I HOH .  ? B HOH 405 ? 1_555 111.7 ? 
68 OD2 ? B ASP 10 ? B ASP 10  ? 1_555 CA ? G CA . ? B CA 303 ? 1_555 O   ? I HOH .  ? B HOH 405 ? 1_555 75.5  ? 
69 O   ? B TYR 12 ? B TYR 12  ? 1_555 CA ? G CA . ? B CA 303 ? 1_555 O   ? I HOH .  ? B HOH 405 ? 1_555 170.4 ? 
70 OD1 ? B ASN 14 ? B ASN 14  ? 1_555 CA ? G CA . ? B CA 303 ? 1_555 O   ? I HOH .  ? B HOH 405 ? 1_555 89.7  ? 
71 OD2 ? B ASP 19 ? B ASP 19  ? 1_555 CA ? G CA . ? B CA 303 ? 1_555 O   ? I HOH .  ? B HOH 405 ? 1_555 83.3  ? 
72 O   ? I HOH .  ? B HOH 404 ? 1_555 CA ? G CA . ? B CA 303 ? 1_555 O   ? I HOH .  ? B HOH 405 ? 1_555 91.3  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ALA 207 A . ? ALA 207 A ASP 208 A ? ASP 208 A 1 3.29 
2 ALA 207 B . ? ALA 207 B ASP 208 B ? ASP 208 B 1 3.97 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 6 ? 
AA3 ? 6 ? 
AA4 ? 7 ? 
AA5 ? 7 ? 
AA6 ? 6 ? 
AA7 ? 6 ? 
AA8 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA5 6 7 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA7 5 6 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA8 5 6 ? anti-parallel 
AA8 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LYS A 36  ? LYS A 39  ? LYS A 36  LYS A 39  
AA1 2 HIS A 24  ? ILE A 29  ? HIS A 24  ILE A 29  
AA1 3 ILE A 4   ? ASP A 10  ? ILE A 4   ASP A 10  
AA1 4 GLY A 209 ? SER A 215 ? GLY A 209 SER A 215 
AA1 5 TRP A 88  ? SER A 96  ? TRP A 88  SER A 96  
AA1 6 VAL A 170 ? PHE A 175 ? VAL A 170 PHE A 175 
AA1 7 LEU A 140 ? GLY A 144 ? LEU A 140 GLY A 144 
AA2 1 LYS A 36  ? LYS A 39  ? LYS A 36  LYS A 39  
AA2 2 HIS A 24  ? ILE A 29  ? HIS A 24  ILE A 29  
AA2 3 ILE A 4   ? ASP A 10  ? ILE A 4   ASP A 10  
AA2 4 GLY A 209 ? SER A 215 ? GLY A 209 SER A 215 
AA2 5 TRP A 88  ? SER A 96  ? TRP A 88  SER A 96  
AA2 6 VAL A 179 ? HIS A 180 ? VAL A 179 HIS A 180 
AA3 1 ALA A 73  ? ASP A 78  ? ALA A 73  ASP A 78  
AA3 2 ARG A 60  ? SER A 66  ? ARG A 60  SER A 66  
AA3 3 VAL A 47  ? ASN A 55  ? VAL A 47  ASN A 55  
AA3 4 ALA A 186 ? LEU A 198 ? ALA A 186 LEU A 198 
AA3 5 THR A 105 ? SER A 117 ? THR A 105 SER A 117 
AA3 6 THR A 123 ? PHE A 130 ? THR A 123 PHE A 130 
AA4 1 ALA A 73  ? ASP A 78  ? ALA A 73  ASP A 78  
AA4 2 ARG A 60  ? SER A 66  ? ARG A 60  SER A 66  
AA4 3 VAL A 47  ? ASN A 55  ? VAL A 47  ASN A 55  
AA4 4 ALA A 186 ? LEU A 198 ? ALA A 186 LEU A 198 
AA4 5 THR A 105 ? SER A 117 ? THR A 105 SER A 117 
AA4 6 LEU A 154 ? GLU A 155 ? LEU A 154 GLU A 155 
AA4 7 THR A 147 ? THR A 148 ? THR A 147 THR A 148 
AA5 1 LYS B 36  ? LYS B 39  ? LYS B 36  LYS B 39  
AA5 2 HIS B 24  ? ILE B 29  ? HIS B 24  ILE B 29  
AA5 3 ILE B 4   ? ASP B 10  ? ILE B 4   ASP B 10  
AA5 4 GLY B 209 ? SER B 215 ? GLY B 209 SER B 215 
AA5 5 TRP B 88  ? SER B 96  ? TRP B 88  SER B 96  
AA5 6 VAL B 170 ? PHE B 175 ? VAL B 170 PHE B 175 
AA5 7 LEU B 140 ? GLY B 144 ? LEU B 140 GLY B 144 
AA6 1 LYS B 36  ? LYS B 39  ? LYS B 36  LYS B 39  
AA6 2 HIS B 24  ? ILE B 29  ? HIS B 24  ILE B 29  
AA6 3 ILE B 4   ? ASP B 10  ? ILE B 4   ASP B 10  
AA6 4 GLY B 209 ? SER B 215 ? GLY B 209 SER B 215 
AA6 5 TRP B 88  ? SER B 96  ? TRP B 88  SER B 96  
AA6 6 VAL B 179 ? HIS B 180 ? VAL B 179 HIS B 180 
AA7 1 ALA B 73  ? ASP B 78  ? ALA B 73  ASP B 78  
AA7 2 ARG B 60  ? SER B 66  ? ARG B 60  SER B 66  
AA7 3 VAL B 47  ? ASN B 55  ? VAL B 47  ASN B 55  
AA7 4 VAL B 188 ? LEU B 198 ? VAL B 188 LEU B 198 
AA7 5 THR B 105 ? LYS B 116 ? THR B 105 LYS B 116 
AA7 6 ASN B 124 ? PHE B 130 ? ASN B 124 PHE B 130 
AA8 1 ALA B 73  ? ASP B 78  ? ALA B 73  ASP B 78  
AA8 2 ARG B 60  ? SER B 66  ? ARG B 60  SER B 66  
AA8 3 VAL B 47  ? ASN B 55  ? VAL B 47  ASN B 55  
AA8 4 VAL B 188 ? LEU B 198 ? VAL B 188 LEU B 198 
AA8 5 THR B 105 ? LYS B 116 ? THR B 105 LYS B 116 
AA8 6 ASN B 153 ? GLU B 155 ? ASN B 153 GLU B 155 
AA8 7 THR B 147 ? THR B 150 ? THR B 147 THR B 150 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 38  ? O ALA A 38  N ILE A 25  ? N ILE A 25  
AA1 2 3 O ASP A 28  ? O ASP A 28  N ALA A 6   ? N ALA A 6   
AA1 3 4 N LEU A 9   ? N LEU A 9   O ILE A 210 ? O ILE A 210 
AA1 4 5 O PHE A 213 ? O PHE A 213 N GLY A 92  ? N GLY A 92  
AA1 5 6 N LEU A 93  ? N LEU A 93  O ALA A 173 ? O ALA A 173 
AA1 6 7 O LEU A 174 ? O LEU A 174 N ILE A 141 ? N ILE A 141 
AA2 1 2 O ALA A 38  ? O ALA A 38  N ILE A 25  ? N ILE A 25  
AA2 2 3 O ASP A 28  ? O ASP A 28  N ALA A 6   ? N ALA A 6   
AA2 3 4 N LEU A 9   ? N LEU A 9   O ILE A 210 ? O ILE A 210 
AA2 4 5 O PHE A 213 ? O PHE A 213 N GLY A 92  ? N GLY A 92  
AA2 5 6 N VAL A 89  ? N VAL A 89  O VAL A 179 ? O VAL A 179 
AA3 1 2 O ALA A 73  ? O ALA A 73  N VAL A 65  ? N VAL A 65  
AA3 2 3 O SER A 62  ? O SER A 62  N ILE A 53  ? N ILE A 53  
AA3 3 4 N GLY A 48  ? N GLY A 48  O PHE A 197 ? O PHE A 197 
AA3 4 5 O VAL A 187 ? O VAL A 187 N LYS A 116 ? N LYS A 116 
AA3 5 6 N TRP A 109 ? N TRP A 109 O PHE A 130 ? O PHE A 130 
AA4 1 2 O ALA A 73  ? O ALA A 73  N VAL A 65  ? N VAL A 65  
AA4 2 3 O SER A 62  ? O SER A 62  N ILE A 53  ? N ILE A 53  
AA4 3 4 N GLY A 48  ? N GLY A 48  O PHE A 197 ? O PHE A 197 
AA4 4 5 O VAL A 187 ? O VAL A 187 N LYS A 116 ? N LYS A 116 
AA4 5 6 N ILE A 106 ? N ILE A 106 O LEU A 154 ? O LEU A 154 
AA4 6 7 O GLU A 155 ? O GLU A 155 N THR A 147 ? N THR A 147 
AA5 1 2 O LYS B 36  ? O LYS B 36  N ILE B 27  ? N ILE B 27  
AA5 2 3 O ASP B 28  ? O ASP B 28  N ALA B 6   ? N ALA B 6   
AA5 3 4 N LEU B 9   ? N LEU B 9   O ILE B 210 ? O ILE B 210 
AA5 4 5 O ALA B 211 ? O ALA B 211 N SER B 94  ? N SER B 94  
AA5 5 6 N VAL B 91  ? N VAL B 91  O PHE B 175 ? O PHE B 175 
AA5 6 7 O ARG B 172 ? O ARG B 172 N GLN B 143 ? N GLN B 143 
AA6 1 2 O LYS B 36  ? O LYS B 36  N ILE B 27  ? N ILE B 27  
AA6 2 3 O ASP B 28  ? O ASP B 28  N ALA B 6   ? N ALA B 6   
AA6 3 4 N LEU B 9   ? N LEU B 9   O ILE B 210 ? O ILE B 210 
AA6 4 5 O ALA B 211 ? O ALA B 211 N SER B 94  ? N SER B 94  
AA6 5 6 N VAL B 89  ? N VAL B 89  O VAL B 179 ? O VAL B 179 
AA7 1 2 O ALA B 73  ? O ALA B 73  N VAL B 65  ? N VAL B 65  
AA7 2 3 O SER B 66  ? O SER B 66  N THR B 49  ? N THR B 49  
AA7 3 4 N ILE B 52  ? N ILE B 52  O ALA B 193 ? O ALA B 193 
AA7 4 5 O VAL B 188 ? O VAL B 188 N LYS B 116 ? N LYS B 116 
AA7 5 6 N TRP B 109 ? N TRP B 109 O PHE B 130 ? O PHE B 130 
AA8 1 2 O ALA B 73  ? O ALA B 73  N VAL B 65  ? N VAL B 65  
AA8 2 3 O SER B 66  ? O SER B 66  N THR B 49  ? N THR B 49  
AA8 3 4 N ILE B 52  ? N ILE B 52  O ALA B 193 ? O ALA B 193 
AA8 4 5 O VAL B 188 ? O VAL B 188 N LYS B 116 ? N LYS B 116 
AA8 5 6 N ILE B 106 ? N ILE B 106 O LEU B 154 ? O LEU B 154 
AA8 6 7 O GLU B 155 ? O GLU B 155 N THR B 147 ? N THR B 147 
# 
_pdbx_entry_details.entry_id                   9J1B 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 104 ? ? -119.29 69.67   
2 1 GLU A 183 ? ? -164.80 119.08  
3 1 ASN B 69  ? ? 71.26   32.57   
4 1 ASN B 104 ? ? -115.32 65.02   
5 1 SER B 117 ? ? -149.54 -157.38 
6 1 THR B 120 ? ? -156.58 -104.54 
7 1 LEU B 230 ? ? 59.85   17.24   
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1EAT C12  C  Y N 1   
A1EAT C14  C  Y N 2   
A1EAT C15  C  N N 3   
A1EAT C9   C  Y N 4   
A1EAT C10  C  Y N 5   
A1EAT C11  C  Y N 6   
A1EAT C13  C  Y N 7   
A1EAT O7   O  N N 8   
A1EAT C24  C  N N 9   
A1EAT CG   C  Y N 10  
A1EAT CD2  C  Y N 11  
A1EAT NE2  N  Y N 12  
A1EAT CE1  C  Y N 13  
A1EAT ND1  N  Y N 14  
A1EAT C    C  Y N 15  
A1EAT C1   C  Y N 16  
A1EAT C2   C  Y N 17  
A1EAT C3   C  Y N 18  
A1EAT C4   C  Y N 19  
A1EAT C5   C  Y N 20  
A1EAT O    O  N N 21  
A1EAT C16  C  N N 22  
A1EAT N2   N  N N 23  
A1EAT C23  C  N N 24  
A1EAT O1M  O  N N 25  
A1EAT C1M  C  N S 26  
A1EAT C2M  C  N S 27  
A1EAT C3M  C  N S 28  
A1EAT C4M  C  N S 29  
A1EAT C5M  C  N R 30  
A1EAT C6M  C  N N 31  
A1EAT O2M  O  N N 32  
A1EAT O3M  O  N N 33  
A1EAT O4M  O  N N 34  
A1EAT O5M  O  N N 35  
A1EAT O6M  O  N N 36  
A1EAT C25  C  N N 37  
A1EAT N3   N  N N 38  
A1EAT C32  C  N N 39  
A1EAT O1M2 O  N N 40  
A1EAT C1M2 C  N S 41  
A1EAT C2M2 C  N S 42  
A1EAT C3M2 C  N S 43  
A1EAT C4M2 C  N S 44  
A1EAT C5M2 C  N R 45  
A1EAT C6M2 C  N N 46  
A1EAT O2M2 O  N N 47  
A1EAT O3M2 O  N N 48  
A1EAT O4M2 O  N N 49  
A1EAT O5M2 O  N N 50  
A1EAT O6M2 O  N N 51  
A1EAT H1   H  N N 52  
A1EAT H4   H  N N 53  
A1EAT H5   H  N N 54  
A1EAT H6   H  N N 55  
A1EAT H23  H  N N 56  
A1EAT H24  H  N N 57  
A1EAT H25  H  N N 58  
A1EAT H26  H  N N 59  
A1EAT H27  H  N N 60  
A1EAT H28  H  N N 61  
A1EAT H29  H  N N 62  
A1EAT H2   H  N N 63  
A1EAT H3   H  N N 64  
A1EAT H30  H  N N 65  
A1EAT H31  H  N N 66  
A1EAT H32  H  N N 67  
A1EAT H33  H  N N 68  
A1EAT H42  H  N N 69  
A1EAT H40  H  N N 70  
A1EAT H38  H  N N 71  
A1EAT H34  H  N N 72  
A1EAT H35  H  N N 73  
A1EAT H36  H  N N 74  
A1EAT H43  H  N N 75  
A1EAT H41  H  N N 76  
A1EAT H39  H  N N 77  
A1EAT H37  H  N N 78  
A1EAT H8   H  N N 79  
A1EAT H9   H  N N 80  
A1EAT H7   H  N N 81  
A1EAT H10  H  N N 82  
A1EAT H11  H  N N 83  
A1EAT H12  H  N N 84  
A1EAT H21  H  N N 85  
A1EAT H19  H  N N 86  
A1EAT H17  H  N N 87  
A1EAT H13  H  N N 88  
A1EAT H14  H  N N 89  
A1EAT H15  H  N N 90  
A1EAT H22  H  N N 91  
A1EAT H20  H  N N 92  
A1EAT H18  H  N N 93  
A1EAT H16  H  N N 94  
ALA   N    N  N N 95  
ALA   CA   C  N S 96  
ALA   C    C  N N 97  
ALA   O    O  N N 98  
ALA   CB   C  N N 99  
ALA   OXT  O  N N 100 
ALA   H    H  N N 101 
ALA   H2   H  N N 102 
ALA   HA   H  N N 103 
ALA   HB1  H  N N 104 
ALA   HB2  H  N N 105 
ALA   HB3  H  N N 106 
ALA   HXT  H  N N 107 
ARG   N    N  N N 108 
ARG   CA   C  N S 109 
ARG   C    C  N N 110 
ARG   O    O  N N 111 
ARG   CB   C  N N 112 
ARG   CG   C  N N 113 
ARG   CD   C  N N 114 
ARG   NE   N  N N 115 
ARG   CZ   C  N N 116 
ARG   NH1  N  N N 117 
ARG   NH2  N  N N 118 
ARG   OXT  O  N N 119 
ARG   H    H  N N 120 
ARG   H2   H  N N 121 
ARG   HA   H  N N 122 
ARG   HB2  H  N N 123 
ARG   HB3  H  N N 124 
ARG   HG2  H  N N 125 
ARG   HG3  H  N N 126 
ARG   HD2  H  N N 127 
ARG   HD3  H  N N 128 
ARG   HE   H  N N 129 
ARG   HH11 H  N N 130 
ARG   HH12 H  N N 131 
ARG   HH21 H  N N 132 
ARG   HH22 H  N N 133 
ARG   HXT  H  N N 134 
ASN   N    N  N N 135 
ASN   CA   C  N S 136 
ASN   C    C  N N 137 
ASN   O    O  N N 138 
ASN   CB   C  N N 139 
ASN   CG   C  N N 140 
ASN   OD1  O  N N 141 
ASN   ND2  N  N N 142 
ASN   OXT  O  N N 143 
ASN   H    H  N N 144 
ASN   H2   H  N N 145 
ASN   HA   H  N N 146 
ASN   HB2  H  N N 147 
ASN   HB3  H  N N 148 
ASN   HD21 H  N N 149 
ASN   HD22 H  N N 150 
ASN   HXT  H  N N 151 
ASP   N    N  N N 152 
ASP   CA   C  N S 153 
ASP   C    C  N N 154 
ASP   O    O  N N 155 
ASP   CB   C  N N 156 
ASP   CG   C  N N 157 
ASP   OD1  O  N N 158 
ASP   OD2  O  N N 159 
ASP   OXT  O  N N 160 
ASP   H    H  N N 161 
ASP   H2   H  N N 162 
ASP   HA   H  N N 163 
ASP   HB2  H  N N 164 
ASP   HB3  H  N N 165 
ASP   HD2  H  N N 166 
ASP   HXT  H  N N 167 
CA    CA   CA N N 168 
GLN   N    N  N N 169 
GLN   CA   C  N S 170 
GLN   C    C  N N 171 
GLN   O    O  N N 172 
GLN   CB   C  N N 173 
GLN   CG   C  N N 174 
GLN   CD   C  N N 175 
GLN   OE1  O  N N 176 
GLN   NE2  N  N N 177 
GLN   OXT  O  N N 178 
GLN   H    H  N N 179 
GLN   H2   H  N N 180 
GLN   HA   H  N N 181 
GLN   HB2  H  N N 182 
GLN   HB3  H  N N 183 
GLN   HG2  H  N N 184 
GLN   HG3  H  N N 185 
GLN   HE21 H  N N 186 
GLN   HE22 H  N N 187 
GLN   HXT  H  N N 188 
GLU   N    N  N N 189 
GLU   CA   C  N S 190 
GLU   C    C  N N 191 
GLU   O    O  N N 192 
GLU   CB   C  N N 193 
GLU   CG   C  N N 194 
GLU   CD   C  N N 195 
GLU   OE1  O  N N 196 
GLU   OE2  O  N N 197 
GLU   OXT  O  N N 198 
GLU   H    H  N N 199 
GLU   H2   H  N N 200 
GLU   HA   H  N N 201 
GLU   HB2  H  N N 202 
GLU   HB3  H  N N 203 
GLU   HG2  H  N N 204 
GLU   HG3  H  N N 205 
GLU   HE2  H  N N 206 
GLU   HXT  H  N N 207 
GLY   N    N  N N 208 
GLY   CA   C  N N 209 
GLY   C    C  N N 210 
GLY   O    O  N N 211 
GLY   OXT  O  N N 212 
GLY   H    H  N N 213 
GLY   H2   H  N N 214 
GLY   HA2  H  N N 215 
GLY   HA3  H  N N 216 
GLY   HXT  H  N N 217 
HIS   N    N  N N 218 
HIS   CA   C  N S 219 
HIS   C    C  N N 220 
HIS   O    O  N N 221 
HIS   CB   C  N N 222 
HIS   CG   C  Y N 223 
HIS   ND1  N  Y N 224 
HIS   CD2  C  Y N 225 
HIS   CE1  C  Y N 226 
HIS   NE2  N  Y N 227 
HIS   OXT  O  N N 228 
HIS   H    H  N N 229 
HIS   H2   H  N N 230 
HIS   HA   H  N N 231 
HIS   HB2  H  N N 232 
HIS   HB3  H  N N 233 
HIS   HD1  H  N N 234 
HIS   HD2  H  N N 235 
HIS   HE1  H  N N 236 
HIS   HE2  H  N N 237 
HIS   HXT  H  N N 238 
HOH   O    O  N N 239 
HOH   H1   H  N N 240 
HOH   H2   H  N N 241 
ILE   N    N  N N 242 
ILE   CA   C  N S 243 
ILE   C    C  N N 244 
ILE   O    O  N N 245 
ILE   CB   C  N S 246 
ILE   CG1  C  N N 247 
ILE   CG2  C  N N 248 
ILE   CD1  C  N N 249 
ILE   OXT  O  N N 250 
ILE   H    H  N N 251 
ILE   H2   H  N N 252 
ILE   HA   H  N N 253 
ILE   HB   H  N N 254 
ILE   HG12 H  N N 255 
ILE   HG13 H  N N 256 
ILE   HG21 H  N N 257 
ILE   HG22 H  N N 258 
ILE   HG23 H  N N 259 
ILE   HD11 H  N N 260 
ILE   HD12 H  N N 261 
ILE   HD13 H  N N 262 
ILE   HXT  H  N N 263 
LEU   N    N  N N 264 
LEU   CA   C  N S 265 
LEU   C    C  N N 266 
LEU   O    O  N N 267 
LEU   CB   C  N N 268 
LEU   CG   C  N N 269 
LEU   CD1  C  N N 270 
LEU   CD2  C  N N 271 
LEU   OXT  O  N N 272 
LEU   H    H  N N 273 
LEU   H2   H  N N 274 
LEU   HA   H  N N 275 
LEU   HB2  H  N N 276 
LEU   HB3  H  N N 277 
LEU   HG   H  N N 278 
LEU   HD11 H  N N 279 
LEU   HD12 H  N N 280 
LEU   HD13 H  N N 281 
LEU   HD21 H  N N 282 
LEU   HD22 H  N N 283 
LEU   HD23 H  N N 284 
LEU   HXT  H  N N 285 
LYS   N    N  N N 286 
LYS   CA   C  N S 287 
LYS   C    C  N N 288 
LYS   O    O  N N 289 
LYS   CB   C  N N 290 
LYS   CG   C  N N 291 
LYS   CD   C  N N 292 
LYS   CE   C  N N 293 
LYS   NZ   N  N N 294 
LYS   OXT  O  N N 295 
LYS   H    H  N N 296 
LYS   H2   H  N N 297 
LYS   HA   H  N N 298 
LYS   HB2  H  N N 299 
LYS   HB3  H  N N 300 
LYS   HG2  H  N N 301 
LYS   HG3  H  N N 302 
LYS   HD2  H  N N 303 
LYS   HD3  H  N N 304 
LYS   HE2  H  N N 305 
LYS   HE3  H  N N 306 
LYS   HZ1  H  N N 307 
LYS   HZ2  H  N N 308 
LYS   HZ3  H  N N 309 
LYS   HXT  H  N N 310 
MET   N    N  N N 311 
MET   CA   C  N S 312 
MET   C    C  N N 313 
MET   O    O  N N 314 
MET   CB   C  N N 315 
MET   CG   C  N N 316 
MET   SD   S  N N 317 
MET   CE   C  N N 318 
MET   OXT  O  N N 319 
MET   H    H  N N 320 
MET   H2   H  N N 321 
MET   HA   H  N N 322 
MET   HB2  H  N N 323 
MET   HB3  H  N N 324 
MET   HG2  H  N N 325 
MET   HG3  H  N N 326 
MET   HE1  H  N N 327 
MET   HE2  H  N N 328 
MET   HE3  H  N N 329 
MET   HXT  H  N N 330 
MN    MN   MN N N 331 
PHE   N    N  N N 332 
PHE   CA   C  N S 333 
PHE   C    C  N N 334 
PHE   O    O  N N 335 
PHE   CB   C  N N 336 
PHE   CG   C  Y N 337 
PHE   CD1  C  Y N 338 
PHE   CD2  C  Y N 339 
PHE   CE1  C  Y N 340 
PHE   CE2  C  Y N 341 
PHE   CZ   C  Y N 342 
PHE   OXT  O  N N 343 
PHE   H    H  N N 344 
PHE   H2   H  N N 345 
PHE   HA   H  N N 346 
PHE   HB2  H  N N 347 
PHE   HB3  H  N N 348 
PHE   HD1  H  N N 349 
PHE   HD2  H  N N 350 
PHE   HE1  H  N N 351 
PHE   HE2  H  N N 352 
PHE   HZ   H  N N 353 
PHE   HXT  H  N N 354 
PRO   N    N  N N 355 
PRO   CA   C  N S 356 
PRO   C    C  N N 357 
PRO   O    O  N N 358 
PRO   CB   C  N N 359 
PRO   CG   C  N N 360 
PRO   CD   C  N N 361 
PRO   OXT  O  N N 362 
PRO   H    H  N N 363 
PRO   HA   H  N N 364 
PRO   HB2  H  N N 365 
PRO   HB3  H  N N 366 
PRO   HG2  H  N N 367 
PRO   HG3  H  N N 368 
PRO   HD2  H  N N 369 
PRO   HD3  H  N N 370 
PRO   HXT  H  N N 371 
SER   N    N  N N 372 
SER   CA   C  N S 373 
SER   C    C  N N 374 
SER   O    O  N N 375 
SER   CB   C  N N 376 
SER   OG   O  N N 377 
SER   OXT  O  N N 378 
SER   H    H  N N 379 
SER   H2   H  N N 380 
SER   HA   H  N N 381 
SER   HB2  H  N N 382 
SER   HB3  H  N N 383 
SER   HG   H  N N 384 
SER   HXT  H  N N 385 
THR   N    N  N N 386 
THR   CA   C  N S 387 
THR   C    C  N N 388 
THR   O    O  N N 389 
THR   CB   C  N R 390 
THR   OG1  O  N N 391 
THR   CG2  C  N N 392 
THR   OXT  O  N N 393 
THR   H    H  N N 394 
THR   H2   H  N N 395 
THR   HA   H  N N 396 
THR   HB   H  N N 397 
THR   HG1  H  N N 398 
THR   HG21 H  N N 399 
THR   HG22 H  N N 400 
THR   HG23 H  N N 401 
THR   HXT  H  N N 402 
TRP   N    N  N N 403 
TRP   CA   C  N S 404 
TRP   C    C  N N 405 
TRP   O    O  N N 406 
TRP   CB   C  N N 407 
TRP   CG   C  Y N 408 
TRP   CD1  C  Y N 409 
TRP   CD2  C  Y N 410 
TRP   NE1  N  Y N 411 
TRP   CE2  C  Y N 412 
TRP   CE3  C  Y N 413 
TRP   CZ2  C  Y N 414 
TRP   CZ3  C  Y N 415 
TRP   CH2  C  Y N 416 
TRP   OXT  O  N N 417 
TRP   H    H  N N 418 
TRP   H2   H  N N 419 
TRP   HA   H  N N 420 
TRP   HB2  H  N N 421 
TRP   HB3  H  N N 422 
TRP   HD1  H  N N 423 
TRP   HE1  H  N N 424 
TRP   HE3  H  N N 425 
TRP   HZ2  H  N N 426 
TRP   HZ3  H  N N 427 
TRP   HH2  H  N N 428 
TRP   HXT  H  N N 429 
TYR   N    N  N N 430 
TYR   CA   C  N S 431 
TYR   C    C  N N 432 
TYR   O    O  N N 433 
TYR   CB   C  N N 434 
TYR   CG   C  Y N 435 
TYR   CD1  C  Y N 436 
TYR   CD2  C  Y N 437 
TYR   CE1  C  Y N 438 
TYR   CE2  C  Y N 439 
TYR   CZ   C  Y N 440 
TYR   OH   O  N N 441 
TYR   OXT  O  N N 442 
TYR   H    H  N N 443 
TYR   H2   H  N N 444 
TYR   HA   H  N N 445 
TYR   HB2  H  N N 446 
TYR   HB3  H  N N 447 
TYR   HD1  H  N N 448 
TYR   HD2  H  N N 449 
TYR   HE1  H  N N 450 
TYR   HE2  H  N N 451 
TYR   HH   H  N N 452 
TYR   HXT  H  N N 453 
VAL   N    N  N N 454 
VAL   CA   C  N S 455 
VAL   C    C  N N 456 
VAL   O    O  N N 457 
VAL   CB   C  N N 458 
VAL   CG1  C  N N 459 
VAL   CG2  C  N N 460 
VAL   OXT  O  N N 461 
VAL   H    H  N N 462 
VAL   H2   H  N N 463 
VAL   HA   H  N N 464 
VAL   HB   H  N N 465 
VAL   HG11 H  N N 466 
VAL   HG12 H  N N 467 
VAL   HG13 H  N N 468 
VAL   HG21 H  N N 469 
VAL   HG22 H  N N 470 
VAL   HG23 H  N N 471 
VAL   HXT  H  N N 472 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1EAT O6M  C6M  sing N N 1   
A1EAT C6M  C5M  sing N N 2   
A1EAT O2M  C2M  sing N N 3   
A1EAT O5M  C5M  sing N N 4   
A1EAT O5M  C1M  sing N N 5   
A1EAT C4M  C5M  sing N N 6   
A1EAT C4M  O4M  sing N N 7   
A1EAT C4M  C3M  sing N N 8   
A1EAT O3M  C3M  sing N N 9   
A1EAT C2M  C3M  sing N N 10  
A1EAT C2M  C1M  sing N N 11  
A1EAT C1M  O1M  sing N N 12  
A1EAT O1M  C23  sing N N 13  
A1EAT C23  C16  sing N N 14  
A1EAT C16  N2   sing N N 15  
A1EAT N2   C15  sing N N 16  
A1EAT O    C15  doub N N 17  
A1EAT C15  C    sing N N 18  
A1EAT C    C1   doub Y N 19  
A1EAT C    C5   sing Y N 20  
A1EAT C1   C2   sing Y N 21  
A1EAT C5   C4   doub Y N 22  
A1EAT C2   C3   doub Y N 23  
A1EAT C4   C3   sing Y N 24  
A1EAT C3   NE2  sing N N 25  
A1EAT NE2  CE1  sing Y N 26  
A1EAT NE2  CD2  sing Y N 27  
A1EAT CE1  ND1  doub Y N 28  
A1EAT CD2  CG   doub Y N 29  
A1EAT ND1  CG   sing Y N 30  
A1EAT ND1  C9   sing N N 31  
A1EAT C10  C9   doub Y N 32  
A1EAT C10  C11  sing Y N 33  
A1EAT C9   C14  sing Y N 34  
A1EAT C11  C12  doub Y N 35  
A1EAT C14  C13  doub Y N 36  
A1EAT C12  C13  sing Y N 37  
A1EAT C12  C24  sing N N 38  
A1EAT C24  N3   sing N N 39  
A1EAT C24  O7   doub N N 40  
A1EAT N3   C25  sing N N 41  
A1EAT C25  C32  sing N N 42  
A1EAT C32  O1M2 sing N N 43  
A1EAT O1M2 C1M2 sing N N 44  
A1EAT C3M2 O3M2 sing N N 45  
A1EAT C3M2 C2M2 sing N N 46  
A1EAT C3M2 C4M2 sing N N 47  
A1EAT C1M2 C2M2 sing N N 48  
A1EAT C1M2 O5M2 sing N N 49  
A1EAT O4M2 C4M2 sing N N 50  
A1EAT C2M2 O2M2 sing N N 51  
A1EAT C5M2 C4M2 sing N N 52  
A1EAT C5M2 O5M2 sing N N 53  
A1EAT C5M2 C6M2 sing N N 54  
A1EAT C6M2 O6M2 sing N N 55  
A1EAT C14  H1   sing N N 56  
A1EAT C16  H2   sing N N 57  
A1EAT C16  H3   sing N N 58  
A1EAT C10  H4   sing N N 59  
A1EAT C11  H5   sing N N 60  
A1EAT C13  H6   sing N N 61  
A1EAT N3   H7   sing N N 62  
A1EAT C25  H8   sing N N 63  
A1EAT C25  H9   sing N N 64  
A1EAT C32  H10  sing N N 65  
A1EAT C32  H11  sing N N 66  
A1EAT C1M2 H12  sing N N 67  
A1EAT C5M2 H13  sing N N 68  
A1EAT C6M2 H14  sing N N 69  
A1EAT C6M2 H15  sing N N 70  
A1EAT O6M2 H16  sing N N 71  
A1EAT C4M2 H17  sing N N 72  
A1EAT O4M2 H18  sing N N 73  
A1EAT C3M2 H19  sing N N 74  
A1EAT O3M2 H20  sing N N 75  
A1EAT C2M2 H21  sing N N 76  
A1EAT O2M2 H22  sing N N 77  
A1EAT CG   H23  sing N N 78  
A1EAT CD2  H24  sing N N 79  
A1EAT CE1  H25  sing N N 80  
A1EAT C1   H26  sing N N 81  
A1EAT C2   H27  sing N N 82  
A1EAT C4   H28  sing N N 83  
A1EAT C5   H29  sing N N 84  
A1EAT N2   H30  sing N N 85  
A1EAT C23  H31  sing N N 86  
A1EAT C23  H32  sing N N 87  
A1EAT C1M  H33  sing N N 88  
A1EAT C5M  H34  sing N N 89  
A1EAT C6M  H35  sing N N 90  
A1EAT C6M  H36  sing N N 91  
A1EAT O6M  H37  sing N N 92  
A1EAT C4M  H38  sing N N 93  
A1EAT O4M  H39  sing N N 94  
A1EAT C3M  H40  sing N N 95  
A1EAT O3M  H41  sing N N 96  
A1EAT C2M  H42  sing N N 97  
A1EAT O2M  H43  sing N N 98  
ALA   N    CA   sing N N 99  
ALA   N    H    sing N N 100 
ALA   N    H2   sing N N 101 
ALA   CA   C    sing N N 102 
ALA   CA   CB   sing N N 103 
ALA   CA   HA   sing N N 104 
ALA   C    O    doub N N 105 
ALA   C    OXT  sing N N 106 
ALA   CB   HB1  sing N N 107 
ALA   CB   HB2  sing N N 108 
ALA   CB   HB3  sing N N 109 
ALA   OXT  HXT  sing N N 110 
ARG   N    CA   sing N N 111 
ARG   N    H    sing N N 112 
ARG   N    H2   sing N N 113 
ARG   CA   C    sing N N 114 
ARG   CA   CB   sing N N 115 
ARG   CA   HA   sing N N 116 
ARG   C    O    doub N N 117 
ARG   C    OXT  sing N N 118 
ARG   CB   CG   sing N N 119 
ARG   CB   HB2  sing N N 120 
ARG   CB   HB3  sing N N 121 
ARG   CG   CD   sing N N 122 
ARG   CG   HG2  sing N N 123 
ARG   CG   HG3  sing N N 124 
ARG   CD   NE   sing N N 125 
ARG   CD   HD2  sing N N 126 
ARG   CD   HD3  sing N N 127 
ARG   NE   CZ   sing N N 128 
ARG   NE   HE   sing N N 129 
ARG   CZ   NH1  sing N N 130 
ARG   CZ   NH2  doub N N 131 
ARG   NH1  HH11 sing N N 132 
ARG   NH1  HH12 sing N N 133 
ARG   NH2  HH21 sing N N 134 
ARG   NH2  HH22 sing N N 135 
ARG   OXT  HXT  sing N N 136 
ASN   N    CA   sing N N 137 
ASN   N    H    sing N N 138 
ASN   N    H2   sing N N 139 
ASN   CA   C    sing N N 140 
ASN   CA   CB   sing N N 141 
ASN   CA   HA   sing N N 142 
ASN   C    O    doub N N 143 
ASN   C    OXT  sing N N 144 
ASN   CB   CG   sing N N 145 
ASN   CB   HB2  sing N N 146 
ASN   CB   HB3  sing N N 147 
ASN   CG   OD1  doub N N 148 
ASN   CG   ND2  sing N N 149 
ASN   ND2  HD21 sing N N 150 
ASN   ND2  HD22 sing N N 151 
ASN   OXT  HXT  sing N N 152 
ASP   N    CA   sing N N 153 
ASP   N    H    sing N N 154 
ASP   N    H2   sing N N 155 
ASP   CA   C    sing N N 156 
ASP   CA   CB   sing N N 157 
ASP   CA   HA   sing N N 158 
ASP   C    O    doub N N 159 
ASP   C    OXT  sing N N 160 
ASP   CB   CG   sing N N 161 
ASP   CB   HB2  sing N N 162 
ASP   CB   HB3  sing N N 163 
ASP   CG   OD1  doub N N 164 
ASP   CG   OD2  sing N N 165 
ASP   OD2  HD2  sing N N 166 
ASP   OXT  HXT  sing N N 167 
GLN   N    CA   sing N N 168 
GLN   N    H    sing N N 169 
GLN   N    H2   sing N N 170 
GLN   CA   C    sing N N 171 
GLN   CA   CB   sing N N 172 
GLN   CA   HA   sing N N 173 
GLN   C    O    doub N N 174 
GLN   C    OXT  sing N N 175 
GLN   CB   CG   sing N N 176 
GLN   CB   HB2  sing N N 177 
GLN   CB   HB3  sing N N 178 
GLN   CG   CD   sing N N 179 
GLN   CG   HG2  sing N N 180 
GLN   CG   HG3  sing N N 181 
GLN   CD   OE1  doub N N 182 
GLN   CD   NE2  sing N N 183 
GLN   NE2  HE21 sing N N 184 
GLN   NE2  HE22 sing N N 185 
GLN   OXT  HXT  sing N N 186 
GLU   N    CA   sing N N 187 
GLU   N    H    sing N N 188 
GLU   N    H2   sing N N 189 
GLU   CA   C    sing N N 190 
GLU   CA   CB   sing N N 191 
GLU   CA   HA   sing N N 192 
GLU   C    O    doub N N 193 
GLU   C    OXT  sing N N 194 
GLU   CB   CG   sing N N 195 
GLU   CB   HB2  sing N N 196 
GLU   CB   HB3  sing N N 197 
GLU   CG   CD   sing N N 198 
GLU   CG   HG2  sing N N 199 
GLU   CG   HG3  sing N N 200 
GLU   CD   OE1  doub N N 201 
GLU   CD   OE2  sing N N 202 
GLU   OE2  HE2  sing N N 203 
GLU   OXT  HXT  sing N N 204 
GLY   N    CA   sing N N 205 
GLY   N    H    sing N N 206 
GLY   N    H2   sing N N 207 
GLY   CA   C    sing N N 208 
GLY   CA   HA2  sing N N 209 
GLY   CA   HA3  sing N N 210 
GLY   C    O    doub N N 211 
GLY   C    OXT  sing N N 212 
GLY   OXT  HXT  sing N N 213 
HIS   N    CA   sing N N 214 
HIS   N    H    sing N N 215 
HIS   N    H2   sing N N 216 
HIS   CA   C    sing N N 217 
HIS   CA   CB   sing N N 218 
HIS   CA   HA   sing N N 219 
HIS   C    O    doub N N 220 
HIS   C    OXT  sing N N 221 
HIS   CB   CG   sing N N 222 
HIS   CB   HB2  sing N N 223 
HIS   CB   HB3  sing N N 224 
HIS   CG   ND1  sing Y N 225 
HIS   CG   CD2  doub Y N 226 
HIS   ND1  CE1  doub Y N 227 
HIS   ND1  HD1  sing N N 228 
HIS   CD2  NE2  sing Y N 229 
HIS   CD2  HD2  sing N N 230 
HIS   CE1  NE2  sing Y N 231 
HIS   CE1  HE1  sing N N 232 
HIS   NE2  HE2  sing N N 233 
HIS   OXT  HXT  sing N N 234 
HOH   O    H1   sing N N 235 
HOH   O    H2   sing N N 236 
ILE   N    CA   sing N N 237 
ILE   N    H    sing N N 238 
ILE   N    H2   sing N N 239 
ILE   CA   C    sing N N 240 
ILE   CA   CB   sing N N 241 
ILE   CA   HA   sing N N 242 
ILE   C    O    doub N N 243 
ILE   C    OXT  sing N N 244 
ILE   CB   CG1  sing N N 245 
ILE   CB   CG2  sing N N 246 
ILE   CB   HB   sing N N 247 
ILE   CG1  CD1  sing N N 248 
ILE   CG1  HG12 sing N N 249 
ILE   CG1  HG13 sing N N 250 
ILE   CG2  HG21 sing N N 251 
ILE   CG2  HG22 sing N N 252 
ILE   CG2  HG23 sing N N 253 
ILE   CD1  HD11 sing N N 254 
ILE   CD1  HD12 sing N N 255 
ILE   CD1  HD13 sing N N 256 
ILE   OXT  HXT  sing N N 257 
LEU   N    CA   sing N N 258 
LEU   N    H    sing N N 259 
LEU   N    H2   sing N N 260 
LEU   CA   C    sing N N 261 
LEU   CA   CB   sing N N 262 
LEU   CA   HA   sing N N 263 
LEU   C    O    doub N N 264 
LEU   C    OXT  sing N N 265 
LEU   CB   CG   sing N N 266 
LEU   CB   HB2  sing N N 267 
LEU   CB   HB3  sing N N 268 
LEU   CG   CD1  sing N N 269 
LEU   CG   CD2  sing N N 270 
LEU   CG   HG   sing N N 271 
LEU   CD1  HD11 sing N N 272 
LEU   CD1  HD12 sing N N 273 
LEU   CD1  HD13 sing N N 274 
LEU   CD2  HD21 sing N N 275 
LEU   CD2  HD22 sing N N 276 
LEU   CD2  HD23 sing N N 277 
LEU   OXT  HXT  sing N N 278 
LYS   N    CA   sing N N 279 
LYS   N    H    sing N N 280 
LYS   N    H2   sing N N 281 
LYS   CA   C    sing N N 282 
LYS   CA   CB   sing N N 283 
LYS   CA   HA   sing N N 284 
LYS   C    O    doub N N 285 
LYS   C    OXT  sing N N 286 
LYS   CB   CG   sing N N 287 
LYS   CB   HB2  sing N N 288 
LYS   CB   HB3  sing N N 289 
LYS   CG   CD   sing N N 290 
LYS   CG   HG2  sing N N 291 
LYS   CG   HG3  sing N N 292 
LYS   CD   CE   sing N N 293 
LYS   CD   HD2  sing N N 294 
LYS   CD   HD3  sing N N 295 
LYS   CE   NZ   sing N N 296 
LYS   CE   HE2  sing N N 297 
LYS   CE   HE3  sing N N 298 
LYS   NZ   HZ1  sing N N 299 
LYS   NZ   HZ2  sing N N 300 
LYS   NZ   HZ3  sing N N 301 
LYS   OXT  HXT  sing N N 302 
MET   N    CA   sing N N 303 
MET   N    H    sing N N 304 
MET   N    H2   sing N N 305 
MET   CA   C    sing N N 306 
MET   CA   CB   sing N N 307 
MET   CA   HA   sing N N 308 
MET   C    O    doub N N 309 
MET   C    OXT  sing N N 310 
MET   CB   CG   sing N N 311 
MET   CB   HB2  sing N N 312 
MET   CB   HB3  sing N N 313 
MET   CG   SD   sing N N 314 
MET   CG   HG2  sing N N 315 
MET   CG   HG3  sing N N 316 
MET   SD   CE   sing N N 317 
MET   CE   HE1  sing N N 318 
MET   CE   HE2  sing N N 319 
MET   CE   HE3  sing N N 320 
MET   OXT  HXT  sing N N 321 
PHE   N    CA   sing N N 322 
PHE   N    H    sing N N 323 
PHE   N    H2   sing N N 324 
PHE   CA   C    sing N N 325 
PHE   CA   CB   sing N N 326 
PHE   CA   HA   sing N N 327 
PHE   C    O    doub N N 328 
PHE   C    OXT  sing N N 329 
PHE   CB   CG   sing N N 330 
PHE   CB   HB2  sing N N 331 
PHE   CB   HB3  sing N N 332 
PHE   CG   CD1  doub Y N 333 
PHE   CG   CD2  sing Y N 334 
PHE   CD1  CE1  sing Y N 335 
PHE   CD1  HD1  sing N N 336 
PHE   CD2  CE2  doub Y N 337 
PHE   CD2  HD2  sing N N 338 
PHE   CE1  CZ   doub Y N 339 
PHE   CE1  HE1  sing N N 340 
PHE   CE2  CZ   sing Y N 341 
PHE   CE2  HE2  sing N N 342 
PHE   CZ   HZ   sing N N 343 
PHE   OXT  HXT  sing N N 344 
PRO   N    CA   sing N N 345 
PRO   N    CD   sing N N 346 
PRO   N    H    sing N N 347 
PRO   CA   C    sing N N 348 
PRO   CA   CB   sing N N 349 
PRO   CA   HA   sing N N 350 
PRO   C    O    doub N N 351 
PRO   C    OXT  sing N N 352 
PRO   CB   CG   sing N N 353 
PRO   CB   HB2  sing N N 354 
PRO   CB   HB3  sing N N 355 
PRO   CG   CD   sing N N 356 
PRO   CG   HG2  sing N N 357 
PRO   CG   HG3  sing N N 358 
PRO   CD   HD2  sing N N 359 
PRO   CD   HD3  sing N N 360 
PRO   OXT  HXT  sing N N 361 
SER   N    CA   sing N N 362 
SER   N    H    sing N N 363 
SER   N    H2   sing N N 364 
SER   CA   C    sing N N 365 
SER   CA   CB   sing N N 366 
SER   CA   HA   sing N N 367 
SER   C    O    doub N N 368 
SER   C    OXT  sing N N 369 
SER   CB   OG   sing N N 370 
SER   CB   HB2  sing N N 371 
SER   CB   HB3  sing N N 372 
SER   OG   HG   sing N N 373 
SER   OXT  HXT  sing N N 374 
THR   N    CA   sing N N 375 
THR   N    H    sing N N 376 
THR   N    H2   sing N N 377 
THR   CA   C    sing N N 378 
THR   CA   CB   sing N N 379 
THR   CA   HA   sing N N 380 
THR   C    O    doub N N 381 
THR   C    OXT  sing N N 382 
THR   CB   OG1  sing N N 383 
THR   CB   CG2  sing N N 384 
THR   CB   HB   sing N N 385 
THR   OG1  HG1  sing N N 386 
THR   CG2  HG21 sing N N 387 
THR   CG2  HG22 sing N N 388 
THR   CG2  HG23 sing N N 389 
THR   OXT  HXT  sing N N 390 
TRP   N    CA   sing N N 391 
TRP   N    H    sing N N 392 
TRP   N    H2   sing N N 393 
TRP   CA   C    sing N N 394 
TRP   CA   CB   sing N N 395 
TRP   CA   HA   sing N N 396 
TRP   C    O    doub N N 397 
TRP   C    OXT  sing N N 398 
TRP   CB   CG   sing N N 399 
TRP   CB   HB2  sing N N 400 
TRP   CB   HB3  sing N N 401 
TRP   CG   CD1  doub Y N 402 
TRP   CG   CD2  sing Y N 403 
TRP   CD1  NE1  sing Y N 404 
TRP   CD1  HD1  sing N N 405 
TRP   CD2  CE2  doub Y N 406 
TRP   CD2  CE3  sing Y N 407 
TRP   NE1  CE2  sing Y N 408 
TRP   NE1  HE1  sing N N 409 
TRP   CE2  CZ2  sing Y N 410 
TRP   CE3  CZ3  doub Y N 411 
TRP   CE3  HE3  sing N N 412 
TRP   CZ2  CH2  doub Y N 413 
TRP   CZ2  HZ2  sing N N 414 
TRP   CZ3  CH2  sing Y N 415 
TRP   CZ3  HZ3  sing N N 416 
TRP   CH2  HH2  sing N N 417 
TRP   OXT  HXT  sing N N 418 
TYR   N    CA   sing N N 419 
TYR   N    H    sing N N 420 
TYR   N    H2   sing N N 421 
TYR   CA   C    sing N N 422 
TYR   CA   CB   sing N N 423 
TYR   CA   HA   sing N N 424 
TYR   C    O    doub N N 425 
TYR   C    OXT  sing N N 426 
TYR   CB   CG   sing N N 427 
TYR   CB   HB2  sing N N 428 
TYR   CB   HB3  sing N N 429 
TYR   CG   CD1  doub Y N 430 
TYR   CG   CD2  sing Y N 431 
TYR   CD1  CE1  sing Y N 432 
TYR   CD1  HD1  sing N N 433 
TYR   CD2  CE2  doub Y N 434 
TYR   CD2  HD2  sing N N 435 
TYR   CE1  CZ   doub Y N 436 
TYR   CE1  HE1  sing N N 437 
TYR   CE2  CZ   sing Y N 438 
TYR   CE2  HE2  sing N N 439 
TYR   CZ   OH   sing N N 440 
TYR   OH   HH   sing N N 441 
TYR   OXT  HXT  sing N N 442 
VAL   N    CA   sing N N 443 
VAL   N    H    sing N N 444 
VAL   N    H2   sing N N 445 
VAL   CA   C    sing N N 446 
VAL   CA   CB   sing N N 447 
VAL   CA   HA   sing N N 448 
VAL   C    O    doub N N 449 
VAL   C    OXT  sing N N 450 
VAL   CB   CG1  sing N N 451 
VAL   CB   CG2  sing N N 452 
VAL   CB   HB   sing N N 453 
VAL   CG1  HG11 sing N N 454 
VAL   CG1  HG12 sing N N 455 
VAL   CG1  HG13 sing N N 456 
VAL   CG2  HG21 sing N N 457 
VAL   CG2  HG22 sing N N 458 
VAL   CG2  HG23 sing N N 459 
VAL   OXT  HXT  sing N N 460 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4P9W 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9J1B 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.008519 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006483 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008794 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   -0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.015011 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CA 
MN 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . ALA   A 1 1   ? -24.588 -48.335 12.446  1.00 72.50  ? 1   ALA   A N    1 
ATOM   2    C  CA   . ALA   A 1 1   ? -23.464 -47.519 12.970  1.00 62.51  ? 1   ALA   A CA   1 
ATOM   3    C  C    . ALA   A 1 1   ? -24.022 -46.348 13.793  1.00 62.74  ? 1   ALA   A C    1 
ATOM   4    O  O    . ALA   A 1 1   ? -25.261 -46.059 13.765  1.00 60.57  ? 1   ALA   A O    1 
ATOM   5    C  CB   . ALA   A 1 1   ? -22.588 -47.030 11.833  1.00 54.35  ? 1   ALA   A CB   1 
ATOM   6    N  N    . ASP   A 1 2   ? -23.133 -45.692 14.521  1.00 53.41  ? 2   ASP   A N    1 
ATOM   7    C  CA   . ASP   A 1 2   ? -23.435 -44.435 15.237  1.00 51.78  ? 2   ASP   A CA   1 
ATOM   8    C  C    . ASP   A 1 2   ? -23.869 -43.395 14.190  1.00 52.62  ? 2   ASP   A C    1 
ATOM   9    O  O    . ASP   A 1 2   ? -23.532 -43.585 13.012  1.00 52.33  ? 2   ASP   A O    1 
ATOM   10   C  CB   . ASP   A 1 2   ? -22.225 -44.066 16.094  1.00 57.05  ? 2   ASP   A CB   1 
ATOM   11   C  CG   . ASP   A 1 2   ? -21.823 -45.149 17.091  1.00 62.09  ? 2   ASP   A CG   1 
ATOM   12   O  OD1  . ASP   A 1 2   ? -22.725 -45.896 17.543  1.00 61.69  ? 2   ASP   A OD1  1 
ATOM   13   O  OD2  . ASP   A 1 2   ? -20.614 -45.255 17.397  1.00 67.88  ? 2   ASP   A OD2  1 
ATOM   14   N  N    . THR   A 1 3   ? -24.693 -42.418 14.589  1.00 50.46  ? 3   THR   A N    1 
ATOM   15   C  CA   . THR   A 1 3   ? -24.899 -41.125 13.896  1.00 50.41  ? 3   THR   A CA   1 
ATOM   16   C  C    . THR   A 1 3   ? -23.900 -40.137 14.490  1.00 47.22  ? 3   THR   A C    1 
ATOM   17   O  O    . THR   A 1 3   ? -23.819 -40.079 15.708  1.00 52.87  ? 3   THR   A O    1 
ATOM   18   C  CB   . THR   A 1 3   ? -26.343 -40.634 14.045  1.00 57.12  ? 3   THR   A CB   1 
ATOM   19   O  OG1  . THR   A 1 3   ? -27.174 -41.579 13.374  1.00 59.19  ? 3   THR   A OG1  1 
ATOM   20   C  CG2  . THR   A 1 3   ? -26.597 -39.272 13.438  1.00 56.01  ? 3   THR   A CG2  1 
ATOM   21   N  N    . ILE   A 1 4   ? -23.137 -39.442 13.650  1.00 47.22  ? 4   ILE   A N    1 
ATOM   22   C  CA   . ILE   A 1 4   ? -22.030 -38.533 14.068  1.00 45.51  ? 4   ILE   A CA   1 
ATOM   23   C  C    . ILE   A 1 4   ? -22.167 -37.220 13.302  1.00 44.76  ? 4   ILE   A C    1 
ATOM   24   O  O    . ILE   A 1 4   ? -22.260 -37.295 12.066  1.00 46.63  ? 4   ILE   A O    1 
ATOM   25   C  CB   . ILE   A 1 4   ? -20.637 -39.141 13.812  1.00 44.97  ? 4   ILE   A CB   1 
ATOM   26   C  CG1  . ILE   A 1 4   ? -20.393 -40.414 14.610  1.00 40.89  ? 4   ILE   A CG1  1 
ATOM   27   C  CG2  . ILE   A 1 4   ? -19.583 -38.096 14.144  1.00 50.16  ? 4   ILE   A CG2  1 
ATOM   28   C  CD1  . ILE   A 1 4   ? -20.110 -40.119 16.062  1.00 43.74  ? 4   ILE   A CD1  1 
ATOM   29   N  N    . VAL   A 1 5   ? -22.225 -36.104 14.035  1.00 39.99  ? 5   VAL   A N    1 
ATOM   30   C  CA   . VAL   A 1 5   ? -22.027 -34.713 13.561  1.00 39.76  ? 5   VAL   A CA   1 
ATOM   31   C  C    . VAL   A 1 5   ? -20.762 -34.229 14.271  1.00 47.97  ? 5   VAL   A C    1 
ATOM   32   O  O    . VAL   A 1 5   ? -20.688 -34.381 15.504  1.00 52.62  ? 5   VAL   A O    1 
ATOM   33   C  CB   . VAL   A 1 5   ? -23.255 -33.842 13.871  1.00 43.62  ? 5   VAL   A CB   1 
ATOM   34   C  CG1  . VAL   A 1 5   ? -22.978 -32.349 13.698  1.00 46.43  ? 5   VAL   A CG1  1 
ATOM   35   C  CG2  . VAL   A 1 5   ? -24.482 -34.256 13.054  1.00 41.09  ? 5   VAL   A CG2  1 
ATOM   36   N  N    . ALA   A 1 6   ? -19.741 -33.777 13.541  1.00 43.98  ? 6   ALA   A N    1 
ATOM   37   C  CA   . ALA   A 1 6   ? -18.440 -33.494 14.177  1.00 42.78  ? 6   ALA   A CA   1 
ATOM   38   C  C    . ALA   A 1 6   ? -17.858 -32.231 13.572  1.00 42.59  ? 6   ALA   A C    1 
ATOM   39   O  O    . ALA   A 1 6   ? -18.132 -31.950 12.440  1.00 46.57  ? 6   ALA   A O    1 
ATOM   40   C  CB   . ALA   A 1 6   ? -17.500 -34.651 14.027  1.00 43.84  ? 6   ALA   A CB   1 
ATOM   41   N  N    . VAL   A 1 7   ? -17.090 -31.522 14.370  1.00 37.50  ? 7   VAL   A N    1 
ATOM   42   C  CA   . VAL   A 1 7   ? -16.167 -30.450 13.934  1.00 42.90  ? 7   VAL   A CA   1 
ATOM   43   C  C    . VAL   A 1 7   ? -14.783 -31.040 14.135  1.00 40.63  ? 7   VAL   A C    1 
ATOM   44   O  O    . VAL   A 1 7   ? -14.484 -31.355 15.281  1.00 38.70  ? 7   VAL   A O    1 
ATOM   45   C  CB   . VAL   A 1 7   ? -16.358 -29.144 14.739  1.00 38.71  ? 7   VAL   A CB   1 
ATOM   46   C  CG1  . VAL   A 1 7   ? -15.325 -28.107 14.354  1.00 40.68  ? 7   VAL   A CG1  1 
ATOM   47   C  CG2  . VAL   A 1 7   ? -17.761 -28.586 14.559  1.00 39.82  ? 7   VAL   A CG2  1 
ATOM   48   N  N    . GLU   A 1 8   ? -13.993 -31.148 13.068  1.00 42.53  ? 8   GLU   A N    1 
ATOM   49   C  CA   . GLU   A 1 8   ? -12.660 -31.799 13.104  1.00 40.52  ? 8   GLU   A CA   1 
ATOM   50   C  C    . GLU   A 1 8   ? -11.565 -30.720 13.018  1.00 45.81  ? 8   GLU   A C    1 
ATOM   51   O  O    . GLU   A 1 8   ? -11.665 -29.797 12.193  1.00 42.19  ? 8   GLU   A O    1 
ATOM   52   C  CB   . GLU   A 1 8   ? -12.558 -32.870 12.019  1.00 41.99  ? 8   GLU   A CB   1 
ATOM   53   C  CG   . GLU   A 1 8   ? -12.637 -32.350 10.589  1.00 44.23  ? 8   GLU   A CG   1 
ATOM   54   C  CD   . GLU   A 1 8   ? -12.204 -33.354 9.521   1.00 41.84  ? 8   GLU   A CD   1 
ATOM   55   O  OE1  . GLU   A 1 8   ? -12.836 -34.424 9.386   1.00 41.27  ? 8   GLU   A OE1  1 
ATOM   56   O  OE2  . GLU   A 1 8   ? -11.231 -33.066 8.826   1.00 44.03  ? 8   GLU   A OE2  1 
ATOM   57   N  N    . LEU   A 1 9   ? -10.591 -30.806 13.922  1.00 40.81  ? 9   LEU   A N    1 
ATOM   58   C  CA   . LEU   A 1 9   ? -9.281  -30.150 13.831  1.00 39.53  ? 9   LEU   A CA   1 
ATOM   59   C  C    . LEU   A 1 9   ? -8.325  -31.220 13.254  1.00 41.42  ? 9   LEU   A C    1 
ATOM   60   O  O    . LEU   A 1 9   ? -7.777  -32.023 14.016  1.00 38.43  ? 9   LEU   A O    1 
ATOM   61   C  CB   . LEU   A 1 9   ? -8.909  -29.685 15.247  1.00 43.47  ? 9   LEU   A CB   1 
ATOM   62   C  CG   . LEU   A 1 9   ? -9.597  -28.422 15.785  1.00 43.70  ? 9   LEU   A CG   1 
ATOM   63   C  CD1  . LEU   A 1 9   ? -11.111 -28.473 15.692  1.00 46.17  ? 9   LEU   A CD1  1 
ATOM   64   C  CD2  . LEU   A 1 9   ? -9.196  -28.162 17.220  1.00 44.46  ? 9   LEU   A CD2  1 
ATOM   65   N  N    . ASP   A 1 10  ? -8.164  -31.260 11.936  1.00 38.57  ? 10  ASP   A N    1 
ATOM   66   C  CA   . ASP   A 1 10  ? -7.487  -32.366 11.199  1.00 41.94  ? 10  ASP   A CA   1 
ATOM   67   C  C    . ASP   A 1 10  ? -6.069  -31.909 10.852  1.00 36.97  ? 10  ASP   A C    1 
ATOM   68   O  O    . ASP   A 1 10  ? -5.939  -31.051 9.958   1.00 37.26  ? 10  ASP   A O    1 
ATOM   69   C  CB   . ASP   A 1 10  ? -8.318  -32.768 9.964   1.00 40.81  ? 10  ASP   A CB   1 
ATOM   70   C  CG   . ASP   A 1 10  ? -7.830  -33.993 9.213   1.00 35.86  ? 10  ASP   A CG   1 
ATOM   71   O  OD1  . ASP   A 1 10  ? -6.727  -34.412 9.463   1.00 37.91  ? 10  ASP   A OD1  1 
ATOM   72   O  OD2  . ASP   A 1 10  ? -8.565  -34.507 8.366   1.00 35.50  ? 10  ASP   A OD2  1 
ATOM   73   N  N    . THR   A 1 11  ? -5.054  -32.463 11.526  1.00 36.53  ? 11  THR   A N    1 
ATOM   74   C  CA   . THR   A 1 11  ? -3.631  -32.022 11.444  1.00 36.35  ? 11  THR   A CA   1 
ATOM   75   C  C    . THR   A 1 11  ? -2.877  -32.709 10.292  1.00 41.88  ? 11  THR   A C    1 
ATOM   76   O  O    . THR   A 1 11  ? -1.704  -32.301 10.065  1.00 48.15  ? 11  THR   A O    1 
ATOM   77   C  CB   . THR   A 1 11  ? -2.918  -32.350 12.757  1.00 36.23  ? 11  THR   A CB   1 
ATOM   78   O  OG1  . THR   A 1 11  ? -3.180  -33.717 13.114  1.00 32.60  ? 11  THR   A OG1  1 
ATOM   79   C  CG2  . THR   A 1 11  ? -3.389  -31.430 13.860  1.00 39.33  ? 11  THR   A CG2  1 
ATOM   80   N  N    . TYR   A 1 12  ? -3.457  -33.760 9.674   1.00 41.83  ? 12  TYR   A N    1 
ATOM   81   C  CA   . TYR   A 1 12  ? -2.775  -34.666 8.705   1.00 45.77  ? 12  TYR   A CA   1 
ATOM   82   C  C    . TYR   A 1 12  ? -3.584  -34.860 7.416   1.00 48.36  ? 12  TYR   A C    1 
ATOM   83   O  O    . TYR   A 1 12  ? -4.709  -35.392 7.461   1.00 43.97  ? 12  TYR   A O    1 
ATOM   84   C  CB   . TYR   A 1 12  ? -2.456  -36.039 9.297   1.00 47.27  ? 12  TYR   A CB   1 
ATOM   85   C  CG   . TYR   A 1 12  ? -1.526  -36.822 8.400   1.00 47.36  ? 12  TYR   A CG   1 
ATOM   86   C  CD1  . TYR   A 1 12  ? -0.179  -36.540 8.368   1.00 42.21  ? 12  TYR   A CD1  1 
ATOM   87   C  CD2  . TYR   A 1 12  ? -2.007  -37.771 7.511   1.00 47.10  ? 12  TYR   A CD2  1 
ATOM   88   C  CE1  . TYR   A 1 12  ? 0.675   -37.198 7.510   1.00 44.41  ? 12  TYR   A CE1  1 
ATOM   89   C  CE2  . TYR   A 1 12  ? -1.165  -38.425 6.631   1.00 43.16  ? 12  TYR   A CE2  1 
ATOM   90   C  CZ   . TYR   A 1 12  ? 0.187   -38.163 6.650   1.00 46.22  ? 12  TYR   A CZ   1 
ATOM   91   O  OH   . TYR   A 1 12  ? 1.042   -38.851 5.826   1.00 46.30  ? 12  TYR   A OH   1 
ATOM   92   N  N    . PRO   A 1 13  ? -2.992  -34.485 6.240   1.00 46.79  ? 13  PRO   A N    1 
ATOM   93   C  CA   . PRO   A 1 13  ? -3.650  -34.544 4.931   1.00 46.46  ? 13  PRO   A CA   1 
ATOM   94   C  C    . PRO   A 1 13  ? -3.678  -35.944 4.310   1.00 45.28  ? 13  PRO   A C    1 
ATOM   95   O  O    . PRO   A 1 13  ? -2.704  -36.379 3.738   1.00 44.77  ? 13  PRO   A O    1 
ATOM   96   C  CB   . PRO   A 1 13  ? -2.820  -33.639 4.022   1.00 54.90  ? 13  PRO   A CB   1 
ATOM   97   C  CG   . PRO   A 1 13  ? -1.844  -32.952 4.948   1.00 59.05  ? 13  PRO   A CG   1 
ATOM   98   C  CD   . PRO   A 1 13  ? -1.647  -33.917 6.098   1.00 51.25  ? 13  PRO   A CD   1 
ATOM   99   N  N    . ASN   A 1 14  ? -4.818  -36.607 4.474   1.00 43.33  ? 14  ASN   A N    1 
ATOM   100  C  CA   . ASN   A 1 14  ? -5.190  -37.868 3.791   1.00 42.29  ? 14  ASN   A CA   1 
ATOM   101  C  C    . ASN   A 1 14  ? -5.866  -37.497 2.463   1.00 41.46  ? 14  ASN   A C    1 
ATOM   102  O  O    . ASN   A 1 14  ? -7.096  -37.657 2.372   1.00 47.68  ? 14  ASN   A O    1 
ATOM   103  C  CB   . ASN   A 1 14  ? -6.085  -38.720 4.705   1.00 41.87  ? 14  ASN   A CB   1 
ATOM   104  C  CG   . ASN   A 1 14  ? -5.513  -38.940 6.091   1.00 43.19  ? 14  ASN   A CG   1 
ATOM   105  O  OD1  . ASN   A 1 14  ? -5.688  -38.130 6.996   1.00 45.37  ? 14  ASN   A OD1  1 
ATOM   106  N  ND2  . ASN   A 1 14  ? -4.801  -40.037 6.258   1.00 48.71  ? 14  ASN   A ND2  1 
ATOM   107  N  N    . THR   A 1 15  ? -5.100  -37.018 1.475   1.00 46.40  ? 15  THR   A N    1 
ATOM   108  C  CA   . THR   A 1 15  ? -5.584  -36.540 0.138   1.00 46.43  ? 15  THR   A CA   1 
ATOM   109  C  C    . THR   A 1 15  ? -6.248  -37.674 -0.657  1.00 47.32  ? 15  THR   A C    1 
ATOM   110  O  O    . THR   A 1 15  ? -7.085  -37.354 -1.510  1.00 45.88  ? 15  THR   A O    1 
ATOM   111  C  CB   . THR   A 1 15  ? -4.447  -35.961 -0.712  1.00 46.83  ? 15  THR   A CB   1 
ATOM   112  O  OG1  . THR   A 1 15  ? -3.499  -37.013 -0.950  1.00 50.46  ? 15  THR   A OG1  1 
ATOM   113  C  CG2  . THR   A 1 15  ? -3.757  -34.804 -0.033  1.00 40.84  ? 15  THR   A CG2  1 
ATOM   114  N  N    . ASP   A 1 16  ? -5.954  -38.945 -0.365  1.00 42.92  ? 16  ASP   A N    1 
ATOM   115  C  CA   . ASP   A 1 16  ? -6.695  -40.064 -1.009  1.00 46.93  ? 16  ASP   A CA   1 
ATOM   116  C  C    . ASP   A 1 16  ? -8.151  -40.151 -0.521  1.00 49.81  ? 16  ASP   A C    1 
ATOM   117  O  O    . ASP   A 1 16  ? -8.917  -40.852 -1.215  1.00 54.71  ? 16  ASP   A O    1 
ATOM   118  C  CB   . ASP   A 1 16  ? -6.049  -41.433 -0.785  1.00 47.31  ? 16  ASP   A CB   1 
ATOM   119  C  CG   . ASP   A 1 16  ? -5.982  -41.886 0.668   1.00 49.35  ? 16  ASP   A CG   1 
ATOM   120  O  OD1  . ASP   A 1 16  ? -5.884  -41.009 1.551   1.00 53.32  ? 16  ASP   A OD1  1 
ATOM   121  O  OD2  . ASP   A 1 16  ? -5.949  -43.117 0.901   1.00 49.65  ? 16  ASP   A OD2  1 
ATOM   122  N  N    . ILE   A 1 17  ? -8.547  -39.543 0.612   1.00 44.30  ? 17  ILE   A N    1 
ATOM   123  C  CA   . ILE   A 1 17  ? -9.988  -39.563 1.029   1.00 44.81  ? 17  ILE   A CA   1 
ATOM   124  C  C    . ILE   A 1 17  ? -10.599 -38.150 1.113   1.00 42.13  ? 17  ILE   A C    1 
ATOM   125  O  O    . ILE   A 1 17  ? -11.467 -37.932 1.957   1.00 46.09  ? 17  ILE   A O    1 
ATOM   126  C  CB   . ILE   A 1 17  ? -10.186 -40.379 2.318   1.00 47.40  ? 17  ILE   A CB   1 
ATOM   127  C  CG1  . ILE   A 1 17  ? -9.683  -39.655 3.562   1.00 47.92  ? 17  ILE   A CG1  1 
ATOM   128  C  CG2  . ILE   A 1 17  ? -9.563  -41.756 2.172   1.00 54.61  ? 17  ILE   A CG2  1 
ATOM   129  C  CD1  . ILE   A 1 17  ? -10.252 -40.211 4.819   1.00 50.14  ? 17  ILE   A CD1  1 
ATOM   130  N  N    . GLY   A 1 18  ? -10.215 -37.227 0.233   1.00 45.19  ? 18  GLY   A N    1 
ATOM   131  C  CA   . GLY   A 1 18  ? -10.891 -35.923 0.073   1.00 41.47  ? 18  GLY   A CA   1 
ATOM   132  C  C    . GLY   A 1 18  ? -10.288 -34.836 0.946   1.00 49.76  ? 18  GLY   A C    1 
ATOM   133  O  O    . GLY   A 1 18  ? -10.758 -33.693 0.819   1.00 46.40  ? 18  GLY   A O    1 
ATOM   134  N  N    . ASP   A 1 19  ? -9.271  -35.124 1.783   1.00 47.55  ? 19  ASP   A N    1 
ATOM   135  C  CA   . ASP   A 1 19  ? -8.622  -34.049 2.587   1.00 48.46  ? 19  ASP   A CA   1 
ATOM   136  C  C    . ASP   A 1 19  ? -7.909  -33.078 1.650   1.00 48.26  ? 19  ASP   A C    1 
ATOM   137  O  O    . ASP   A 1 19  ? -7.304  -33.479 0.673   1.00 45.64  ? 19  ASP   A O    1 
ATOM   138  C  CB   . ASP   A 1 19  ? -7.570  -34.568 3.579   1.00 49.45  ? 19  ASP   A CB   1 
ATOM   139  C  CG   . ASP   A 1 19  ? -8.074  -34.956 4.957   1.00 43.86  ? 19  ASP   A CG   1 
ATOM   140  O  OD1  . ASP   A 1 19  ? -9.266  -34.733 5.229   1.00 44.42  ? 19  ASP   A OD1  1 
ATOM   141  O  OD2  . ASP   A 1 19  ? -7.253  -35.477 5.746   1.00 38.49  ? 19  ASP   A OD2  1 
ATOM   142  N  N    . PRO   A 1 20  ? -7.862  -31.764 1.940   1.00 54.96  ? 20  PRO   A N    1 
ATOM   143  C  CA   . PRO   A 1 20  ? -6.913  -30.900 1.236   1.00 50.97  ? 20  PRO   A CA   1 
ATOM   144  C  C    . PRO   A 1 20  ? -5.480  -31.215 1.726   1.00 58.82  ? 20  PRO   A C    1 
ATOM   145  O  O    . PRO   A 1 20  ? -5.347  -31.973 2.690   1.00 64.63  ? 20  PRO   A O    1 
ATOM   146  C  CB   . PRO   A 1 20  ? -7.428  -29.505 1.598   1.00 50.23  ? 20  PRO   A CB   1 
ATOM   147  C  CG   . PRO   A 1 20  ? -8.050  -29.679 2.987   1.00 51.99  ? 20  PRO   A CG   1 
ATOM   148  C  CD   . PRO   A 1 20  ? -8.653  -31.067 2.972   1.00 52.56  ? 20  PRO   A CD   1 
ATOM   149  N  N    . SER   A 1 21  ? -4.458  -30.641 1.075   1.00 59.16  ? 21  SER   A N    1 
ATOM   150  C  CA   . SER   A 1 21  ? -2.997  -30.908 1.259   1.00 66.38  ? 21  SER   A CA   1 
ATOM   151  C  C    . SER   A 1 21  ? -2.416  -30.311 2.552   1.00 59.34  ? 21  SER   A C    1 
ATOM   152  O  O    . SER   A 1 21  ? -1.226  -30.557 2.815   1.00 68.22  ? 21  SER   A O    1 
ATOM   153  C  CB   . SER   A 1 21  ? -2.205  -30.368 0.097   1.00 66.40  ? 21  SER   A CB   1 
ATOM   154  O  OG   . SER   A 1 21  ? -2.473  -31.118 -1.059  1.00 71.78  ? 21  SER   A OG   1 
ATOM   155  N  N    . TYR   A 1 22  ? -3.196  -29.556 3.319   1.00 53.92  ? 22  TYR   A N    1 
ATOM   156  C  CA   . TYR   A 1 22  ? -2.717  -28.784 4.498   1.00 50.71  ? 22  TYR   A CA   1 
ATOM   157  C  C    . TYR   A 1 22  ? -3.554  -29.146 5.723   1.00 47.45  ? 22  TYR   A C    1 
ATOM   158  O  O    . TYR   A 1 22  ? -4.648  -29.686 5.578   1.00 48.62  ? 22  TYR   A O    1 
ATOM   159  C  CB   . TYR   A 1 22  ? -2.803  -27.289 4.188   1.00 48.14  ? 22  TYR   A CB   1 
ATOM   160  C  CG   . TYR   A 1 22  ? -4.049  -26.867 3.449   1.00 48.69  ? 22  TYR   A CG   1 
ATOM   161  C  CD1  . TYR   A 1 22  ? -5.270  -26.752 4.098   1.00 49.42  ? 22  TYR   A CD1  1 
ATOM   162  C  CD2  . TYR   A 1 22  ? -4.025  -26.621 2.083   1.00 54.00  ? 22  TYR   A CD2  1 
ATOM   163  C  CE1  . TYR   A 1 22  ? -6.417  -26.381 3.416   1.00 52.12  ? 22  TYR   A CE1  1 
ATOM   164  C  CE2  . TYR   A 1 22  ? -5.161  -26.219 1.386   1.00 47.09  ? 22  TYR   A CE2  1 
ATOM   165  C  CZ   . TYR   A 1 22  ? -6.355  -26.088 2.060   1.00 54.99  ? 22  TYR   A CZ   1 
ATOM   166  O  OH   . TYR   A 1 22  ? -7.468  -25.721 1.369   1.00 55.15  ? 22  TYR   A OH   1 
ATOM   167  N  N    . PRO   A 1 23  ? -3.063  -28.889 6.960   1.00 49.53  ? 23  PRO   A N    1 
ATOM   168  C  CA   . PRO   A 1 23  ? -3.918  -28.916 8.146   1.00 46.62  ? 23  PRO   A CA   1 
ATOM   169  C  C    . PRO   A 1 23  ? -5.154  -28.047 7.891   1.00 49.13  ? 23  PRO   A C    1 
ATOM   170  O  O    . PRO   A 1 23  ? -5.039  -26.991 7.285   1.00 42.58  ? 23  PRO   A O    1 
ATOM   171  C  CB   . PRO   A 1 23  ? -3.021  -28.339 9.253   1.00 45.61  ? 23  PRO   A CB   1 
ATOM   172  C  CG   . PRO   A 1 23  ? -1.619  -28.771 8.806   1.00 45.60  ? 23  PRO   A CG   1 
ATOM   173  C  CD   . PRO   A 1 23  ? -1.666  -28.552 7.303   1.00 45.74  ? 23  PRO   A CD   1 
ATOM   174  N  N    . HIS   A 1 24  ? -6.305  -28.542 8.339   1.00 47.67  ? 24  HIS   A N    1 
ATOM   175  C  CA   . HIS   A 1 24  ? -7.627  -27.933 8.102   1.00 46.76  ? 24  HIS   A CA   1 
ATOM   176  C  C    . HIS   A 1 24  ? -8.560  -28.182 9.300   1.00 47.82  ? 24  HIS   A C    1 
ATOM   177  O  O    . HIS   A 1 24  ? -8.300  -29.093 10.115  1.00 46.34  ? 24  HIS   A O    1 
ATOM   178  C  CB   . HIS   A 1 24  ? -8.184  -28.482 6.781   1.00 49.43  ? 24  HIS   A CB   1 
ATOM   179  C  CG   . HIS   A 1 24  ? -8.317  -29.971 6.742   1.00 46.57  ? 24  HIS   A CG   1 
ATOM   180  N  ND1  . HIS   A 1 24  ? -7.223  -30.807 6.585   1.00 46.45  ? 24  HIS   A ND1  1 
ATOM   181  C  CD2  . HIS   A 1 24  ? -9.412  -30.769 6.807   1.00 45.96  ? 24  HIS   A CD2  1 
ATOM   182  C  CE1  . HIS   A 1 24  ? -7.643  -32.064 6.583   1.00 53.08  ? 24  HIS   A CE1  1 
ATOM   183  N  NE2  . HIS   A 1 24  ? -8.989  -32.071 6.734   1.00 44.85  ? 24  HIS   A NE2  1 
ATOM   184  N  N    . ILE   A 1 25  ? -9.626  -27.391 9.376   1.00 46.64  ? 25  ILE   A N    1 
ATOM   185  C  CA   . ILE   A 1 25  ? -10.818 -27.621 10.232  1.00 45.33  ? 25  ILE   A CA   1 
ATOM   186  C  C    . ILE   A 1 25  ? -11.996 -27.919 9.305   1.00 44.54  ? 25  ILE   A C    1 
ATOM   187  O  O    . ILE   A 1 25  ? -11.992 -27.448 8.145   1.00 43.21  ? 25  ILE   A O    1 
ATOM   188  C  CB   . ILE   A 1 25  ? -11.079 -26.406 11.134  1.00 49.28  ? 25  ILE   A CB   1 
ATOM   189  C  CG1  . ILE   A 1 25  ? -11.253 -25.127 10.315  1.00 54.44  ? 25  ILE   A CG1  1 
ATOM   190  C  CG2  . ILE   A 1 25  ? -9.967  -26.266 12.167  1.00 49.64  ? 25  ILE   A CG2  1 
ATOM   191  C  CD1  . ILE   A 1 25  ? -11.960 -24.028 11.066  1.00 62.53  ? 25  ILE   A CD1  1 
ATOM   192  N  N    . GLY   A 1 26  ? -12.979 -28.667 9.792   1.00 39.13  ? 26  GLY   A N    1 
ATOM   193  C  CA   . GLY   A 1 26  ? -13.997 -29.242 8.912   1.00 38.61  ? 26  GLY   A CA   1 
ATOM   194  C  C    . GLY   A 1 26  ? -15.250 -29.542 9.670   1.00 39.48  ? 26  GLY   A C    1 
ATOM   195  O  O    . GLY   A 1 26  ? -15.172 -29.725 10.907  1.00 39.98  ? 26  GLY   A O    1 
ATOM   196  N  N    . ILE   A 1 27  ? -16.368 -29.515 8.950   1.00 40.96  ? 27  ILE   A N    1 
ATOM   197  C  CA   . ILE   A 1 27  ? -17.682 -29.919 9.500   1.00 43.19  ? 27  ILE   A CA   1 
ATOM   198  C  C    . ILE   A 1 27  ? -18.011 -31.263 8.861   1.00 47.53  ? 27  ILE   A C    1 
ATOM   199  O  O    . ILE   A 1 27  ? -18.055 -31.320 7.616   1.00 50.61  ? 27  ILE   A O    1 
ATOM   200  C  CB   . ILE   A 1 27  ? -18.718 -28.810 9.254   1.00 45.30  ? 27  ILE   A CB   1 
ATOM   201  C  CG1  . ILE   A 1 27  ? -18.393 -27.617 10.151  1.00 45.22  ? 27  ILE   A CG1  1 
ATOM   202  C  CG2  . ILE   A 1 27  ? -20.138 -29.312 9.486   1.00 48.92  ? 27  ILE   A CG2  1 
ATOM   203  C  CD1  . ILE   A 1 27  ? -19.106 -26.376 9.791   1.00 50.37  ? 27  ILE   A CD1  1 
ATOM   204  N  N    . ASP   A 1 28  ? -18.159 -32.294 9.693   1.00 44.42  ? 28  ASP   A N    1 
ATOM   205  C  CA   . ASP   A 1 28  ? -18.405 -33.702 9.297   1.00 46.98  ? 28  ASP   A CA   1 
ATOM   206  C  C    . ASP   A 1 28  ? -19.860 -34.060 9.647   1.00 47.01  ? 28  ASP   A C    1 
ATOM   207  O  O    . ASP   A 1 28  ? -20.211 -34.036 10.843  1.00 58.20  ? 28  ASP   A O    1 
ATOM   208  C  CB   . ASP   A 1 28  ? -17.383 -34.634 9.964   1.00 53.29  ? 28  ASP   A CB   1 
ATOM   209  C  CG   . ASP   A 1 28  ? -15.919 -34.294 9.714   1.00 51.63  ? 28  ASP   A CG   1 
ATOM   210  O  OD1  . ASP   A 1 28  ? -15.664 -33.601 8.724   1.00 48.06  ? 28  ASP   A OD1  1 
ATOM   211  O  OD2  . ASP   A 1 28  ? -15.044 -34.725 10.526  1.00 46.43  ? 28  ASP   A OD2  1 
ATOM   212  N  N    . ILE   A 1 29  ? -20.694 -34.303 8.630   1.00 48.87  ? 29  ILE   A N    1 
ATOM   213  C  CA   . ILE   A 1 29  ? -22.087 -34.806 8.770   1.00 48.48  ? 29  ILE   A CA   1 
ATOM   214  C  C    . ILE   A 1 29  ? -22.112 -36.257 8.270   1.00 50.00  ? 29  ILE   A C    1 
ATOM   215  O  O    . ILE   A 1 29  ? -22.097 -36.462 7.075   1.00 54.15  ? 29  ILE   A O    1 
ATOM   216  C  CB   . ILE   A 1 29  ? -23.073 -33.889 8.037   1.00 48.88  ? 29  ILE   A CB   1 
ATOM   217  C  CG1  . ILE   A 1 29  ? -22.742 -32.406 8.250   1.00 53.56  ? 29  ILE   A CG1  1 
ATOM   218  C  CG2  . ILE   A 1 29  ? -24.513 -34.234 8.426   1.00 46.00  ? 29  ILE   A CG2  1 
ATOM   219  C  CD1  . ILE   A 1 29  ? -22.910 -31.896 9.679   1.00 54.98  ? 29  ILE   A CD1  1 
ATOM   220  N  N    . LYS   A 1 30  ? -21.988 -37.216 9.192   1.00 56.74  ? 30  LYS   A N    1 
ATOM   221  C  CA   . LYS   A 1 30  ? -22.113 -38.675 8.957   1.00 58.96  ? 30  LYS   A CA   1 
ATOM   222  C  C    . LYS   A 1 30  ? -21.001 -39.175 8.029   1.00 54.62  ? 30  LYS   A C    1 
ATOM   223  O  O    . LYS   A 1 30  ? -21.098 -40.314 7.586   1.00 49.40  ? 30  LYS   A O    1 
ATOM   224  C  CB   . LYS   A 1 30  ? -23.478 -39.005 8.349   1.00 68.84  ? 30  LYS   A CB   1 
ATOM   225  C  CG   . LYS   A 1 30  ? -24.674 -38.814 9.274   1.00 77.77  ? 30  LYS   A CG   1 
ATOM   226  C  CD   . LYS   A 1 30  ? -26.000 -39.085 8.594   1.00 82.93  ? 30  LYS   A CD   1 
ATOM   227  C  CE   . LYS   A 1 30  ? -27.033 -39.656 9.535   1.00 96.31  ? 30  LYS   A CE   1 
ATOM   228  N  NZ   . LYS   A 1 30  ? -28.276 -40.014 8.815   1.00 99.56  ? 30  LYS   A NZ   1 
ATOM   229  N  N    . SER   A 1 31  ? -19.940 -38.404 7.792   1.00 50.93  ? 31  SER   A N    1 
ATOM   230  C  CA   . SER   A 1 31  ? -18.773 -38.896 7.016   1.00 40.51  ? 31  SER   A CA   1 
ATOM   231  C  C    . SER   A 1 31  ? -17.516 -38.148 7.422   1.00 41.70  ? 31  SER   A C    1 
ATOM   232  O  O    . SER   A 1 31  ? -17.617 -36.964 7.811   1.00 49.47  ? 31  SER   A O    1 
ATOM   233  C  CB   . SER   A 1 31  ? -19.071 -38.790 5.542   1.00 38.67  ? 31  SER   A CB   1 
ATOM   234  O  OG   . SER   A 1 31  ? -17.896 -38.734 4.745   1.00 42.13  ? 31  SER   A OG   1 
ATOM   235  N  N    . VAL   A 1 32  ? -16.368 -38.816 7.309   1.00 42.00  ? 32  VAL   A N    1 
ATOM   236  C  CA   . VAL   A 1 32  ? -15.033 -38.217 7.577   1.00 42.57  ? 32  VAL   A CA   1 
ATOM   237  C  C    . VAL   A 1 32  ? -14.674 -37.255 6.436   1.00 46.59  ? 32  VAL   A C    1 
ATOM   238  O  O    . VAL   A 1 32  ? -13.756 -36.425 6.614   1.00 42.76  ? 32  VAL   A O    1 
ATOM   239  C  CB   . VAL   A 1 32  ? -13.963 -39.307 7.739   1.00 49.08  ? 32  VAL   A CB   1 
ATOM   240  C  CG1  . VAL   A 1 32  ? -13.566 -39.889 6.388   1.00 47.04  ? 32  VAL   A CG1  1 
ATOM   241  C  CG2  . VAL   A 1 32  ? -12.745 -38.787 8.484   1.00 47.35  ? 32  VAL   A CG2  1 
ATOM   242  N  N    . ARG   A 1 33  ? -15.320 -37.397 5.284   1.00 46.36  ? 33  ARG   A N    1 
ATOM   243  C  CA   . ARG   A 1 33  ? -15.155 -36.469 4.146   1.00 45.39  ? 33  ARG   A CA   1 
ATOM   244  C  C    . ARG   A 1 33  ? -15.978 -35.223 4.440   1.00 41.92  ? 33  ARG   A C    1 
ATOM   245  O  O    . ARG   A 1 33  ? -17.152 -35.167 4.058   1.00 54.63  ? 33  ARG   A O    1 
ATOM   246  C  CB   . ARG   A 1 33  ? -15.548 -37.126 2.825   1.00 46.27  ? 33  ARG   A CB   1 
ATOM   247  C  CG   . ARG   A 1 33  ? -14.588 -38.235 2.406   1.00 50.63  ? 33  ARG   A CG   1 
ATOM   248  C  CD   . ARG   A 1 33  ? -15.180 -39.074 1.301   1.00 50.94  ? 33  ARG   A CD   1 
ATOM   249  N  NE   . ARG   A 1 33  ? -14.505 -40.347 1.126   1.00 53.83  ? 33  ARG   A NE   1 
ATOM   250  C  CZ   . ARG   A 1 33  ? -13.686 -40.666 0.120   1.00 46.33  ? 33  ARG   A CZ   1 
ATOM   251  N  NH1  . ARG   A 1 33  ? -13.374 -39.788 -0.808  1.00 46.07  ? 33  ARG   A NH1  1 
ATOM   252  N  NH2  . ARG   A 1 33  ? -13.167 -41.875 0.062   1.00 47.09  ? 33  ARG   A NH2  1 
ATOM   253  N  N    . SER   A 1 34  ? -15.346 -34.267 5.098   1.00 37.10  ? 34  SER   A N    1 
ATOM   254  C  CA   . SER   A 1 34  ? -15.938 -32.976 5.508   1.00 40.50  ? 34  SER   A CA   1 
ATOM   255  C  C    . SER   A 1 34  ? -16.816 -32.409 4.381   1.00 44.47  ? 34  SER   A C    1 
ATOM   256  O  O    . SER   A 1 34  ? -16.363 -32.318 3.241   1.00 45.20  ? 34  SER   A O    1 
ATOM   257  C  CB   . SER   A 1 34  ? -14.849 -32.015 5.881   1.00 43.94  ? 34  SER   A CB   1 
ATOM   258  O  OG   . SER   A 1 34  ? -13.885 -32.599 6.755   1.00 43.39  ? 34  SER   A OG   1 
ATOM   259  N  N    . LYS   A 1 35  ? -18.023 -31.978 4.719   1.00 46.13  ? 35  LYS   A N    1 
ATOM   260  C  CA   . LYS   A 1 35  ? -18.906 -31.162 3.852   1.00 42.53  ? 35  LYS   A CA   1 
ATOM   261  C  C    . LYS   A 1 35  ? -18.311 -29.771 3.620   1.00 42.64  ? 35  LYS   A C    1 
ATOM   262  O  O    . LYS   A 1 35  ? -18.560 -29.232 2.564   1.00 44.63  ? 35  LYS   A O    1 
ATOM   263  C  CB   . LYS   A 1 35  ? -20.279 -31.023 4.502   1.00 42.62  ? 35  LYS   A CB   1 
ATOM   264  C  CG   . LYS   A 1 35  ? -20.995 -32.341 4.753   1.00 43.66  ? 35  LYS   A CG   1 
ATOM   265  C  CD   . LYS   A 1 35  ? -21.013 -33.283 3.587   1.00 43.18  ? 35  LYS   A CD   1 
ATOM   266  C  CE   . LYS   A 1 35  ? -21.902 -34.454 3.907   1.00 51.20  ? 35  LYS   A CE   1 
ATOM   267  N  NZ   . LYS   A 1 35  ? -21.471 -35.687 3.218   1.00 61.10  ? 35  LYS   A NZ   1 
ATOM   268  N  N    . LYS   A 1 36  ? -17.558 -29.212 4.565   1.00 42.81  ? 36  LYS   A N    1 
ATOM   269  C  CA   . LYS   A 1 36  ? -16.863 -27.922 4.377   1.00 43.16  ? 36  LYS   A CA   1 
ATOM   270  C  C    . LYS   A 1 36  ? -15.610 -27.910 5.245   1.00 43.85  ? 36  LYS   A C    1 
ATOM   271  O  O    . LYS   A 1 36  ? -15.654 -28.443 6.373   1.00 50.87  ? 36  LYS   A O    1 
ATOM   272  C  CB   . LYS   A 1 36  ? -17.801 -26.756 4.692   1.00 55.11  ? 36  LYS   A CB   1 
ATOM   273  C  CG   . LYS   A 1 36  ? -17.445 -25.462 3.964   1.00 66.72  ? 36  LYS   A CG   1 
ATOM   274  C  CD   . LYS   A 1 36  ? -18.635 -24.706 3.399   1.00 73.77  ? 36  LYS   A CD   1 
ATOM   275  C  CE   . LYS   A 1 36  ? -18.299 -23.260 3.066   1.00 78.46  ? 36  LYS   A CE   1 
ATOM   276  N  NZ   . LYS   A 1 36  ? -19.439 -22.356 3.338   1.00 69.99  ? 36  LYS   A NZ   1 
ATOM   277  N  N    . THR   A 1 37  ? -14.521 -27.376 4.695   1.00 41.51  ? 37  THR   A N    1 
ATOM   278  C  CA   . THR   A 1 37  ? -13.169 -27.345 5.294   1.00 43.87  ? 37  THR   A CA   1 
ATOM   279  C  C    . THR   A 1 37  ? -12.620 -25.926 5.189   1.00 40.12  ? 37  THR   A C    1 
ATOM   280  O  O    . THR   A 1 37  ? -13.124 -25.170 4.411   1.00 41.48  ? 37  THR   A O    1 
ATOM   281  C  CB   . THR   A 1 37  ? -12.210 -28.327 4.615   1.00 43.45  ? 37  THR   A CB   1 
ATOM   282  O  OG1  . THR   A 1 37  ? -12.023 -27.816 3.307   1.00 53.93  ? 37  THR   A OG1  1 
ATOM   283  C  CG2  . THR   A 1 37  ? -12.742 -29.736 4.513   1.00 49.01  ? 37  THR   A CG2  1 
ATOM   284  N  N    . ALA   A 1 38  ? -11.639 -25.569 6.009   1.00 43.50  ? 38  ALA   A N    1 
ATOM   285  C  CA   . ALA   A 1 38  ? -10.892 -24.303 5.868   1.00 40.72  ? 38  ALA   A CA   1 
ATOM   286  C  C    . ALA   A 1 38  ? -9.501  -24.565 6.411   1.00 41.12  ? 38  ALA   A C    1 
ATOM   287  O  O    . ALA   A 1 38  ? -9.332  -25.520 7.201   1.00 37.19  ? 38  ALA   A O    1 
ATOM   288  C  CB   . ALA   A 1 38  ? -11.562 -23.133 6.549   1.00 40.00  ? 38  ALA   A CB   1 
ATOM   289  N  N    . LYS   A 1 39  ? -8.554  -23.843 5.833   1.00 40.76  ? 39  LYS   A N    1 
ATOM   290  C  CA   . LYS   A 1 39  ? -7.114  -23.997 6.079   1.00 47.08  ? 39  LYS   A CA   1 
ATOM   291  C  C    . LYS   A 1 39  ? -6.905  -23.598 7.535   1.00 46.00  ? 39  LYS   A C    1 
ATOM   292  O  O    . LYS   A 1 39  ? -7.617  -22.725 8.016   1.00 48.01  ? 39  LYS   A O    1 
ATOM   293  C  CB   . LYS   A 1 39  ? -6.350  -23.128 5.079   1.00 48.28  ? 39  LYS   A CB   1 
ATOM   294  C  CG   . LYS   A 1 39  ? -4.831  -23.159 5.173   1.00 54.78  ? 39  LYS   A CG   1 
ATOM   295  C  CD   . LYS   A 1 39  ? -4.197  -22.307 4.070   1.00 70.94  ? 39  LYS   A CD   1 
ATOM   296  C  CE   . LYS   A 1 39  ? -2.967  -22.910 3.430   1.00 75.44  ? 39  LYS   A CE   1 
ATOM   297  N  NZ   . LYS   A 1 39  ? -1.983  -23.326 4.455   1.00 84.49  ? 39  LYS   A NZ   1 
ATOM   298  N  N    . TRP   A 1 40  ? -5.941  -24.219 8.180   1.00 47.52  ? 40  TRP   A N    1 
ATOM   299  C  CA   . TRP   A 1 40  ? -5.678  -24.068 9.619   1.00 45.61  ? 40  TRP   A CA   1 
ATOM   300  C  C    . TRP   A 1 40  ? -4.178  -24.233 9.858   1.00 43.06  ? 40  TRP   A C    1 
ATOM   301  O  O    . TRP   A 1 40  ? -3.695  -25.358 9.714   1.00 48.47  ? 40  TRP   A O    1 
ATOM   302  C  CB   . TRP   A 1 40  ? -6.537  -25.081 10.384  1.00 47.66  ? 40  TRP   A CB   1 
ATOM   303  C  CG   . TRP   A 1 40  ? -6.282  -25.078 11.853  1.00 50.15  ? 40  TRP   A CG   1 
ATOM   304  C  CD1  . TRP   A 1 40  ? -6.139  -23.982 12.644  1.00 46.31  ? 40  TRP   A CD1  1 
ATOM   305  C  CD2  . TRP   A 1 40  ? -6.066  -26.231 12.693  1.00 49.94  ? 40  TRP   A CD2  1 
ATOM   306  N  NE1  . TRP   A 1 40  ? -5.856  -24.375 13.925  1.00 53.05  ? 40  TRP   A NE1  1 
ATOM   307  C  CE2  . TRP   A 1 40  ? -5.828  -25.743 13.992  1.00 47.01  ? 40  TRP   A CE2  1 
ATOM   308  C  CE3  . TRP   A 1 40  ? -6.060  -27.613 12.475  1.00 48.15  ? 40  TRP   A CE3  1 
ATOM   309  C  CZ2  . TRP   A 1 40  ? -5.588  -26.591 15.070  1.00 47.96  ? 40  TRP   A CZ2  1 
ATOM   310  C  CZ3  . TRP   A 1 40  ? -5.810  -28.453 13.534  1.00 48.31  ? 40  TRP   A CZ3  1 
ATOM   311  C  CH2  . TRP   A 1 40  ? -5.567  -27.945 14.812  1.00 48.83  ? 40  TRP   A CH2  1 
ATOM   312  N  N    . ASN   A 1 41  ? -3.524  -23.147 10.270  1.00 47.72  ? 41  ASN   A N    1 
ATOM   313  C  CA   . ASN   A 1 41  ? -2.105  -23.045 10.706  1.00 52.39  ? 41  ASN   A CA   1 
ATOM   314  C  C    . ASN   A 1 41  ? -2.053  -23.515 12.162  1.00 52.50  ? 41  ASN   A C    1 
ATOM   315  O  O    . ASN   A 1 41  ? -1.904  -22.709 13.097  1.00 57.27  ? 41  ASN   A O    1 
ATOM   316  C  CB   . ASN   A 1 41  ? -1.592  -21.638 10.383  1.00 51.51  ? 41  ASN   A CB   1 
ATOM   317  C  CG   . ASN   A 1 41  ? -2.152  -21.205 9.036   1.00 66.23  ? 41  ASN   A CG   1 
ATOM   318  O  OD1  . ASN   A 1 41  ? -2.032  -21.960 8.063   1.00 67.19  ? 41  ASN   A OD1  1 
ATOM   319  N  ND2  . ASN   A 1 41  ? -2.845  -20.065 8.971   1.00 58.86  ? 41  ASN   A ND2  1 
ATOM   320  N  N    . MET   A 1 42  ? -2.231  -24.809 12.348  1.00 55.97  ? 42  MET   A N    1 
ATOM   321  C  CA   . MET   A 1 42  ? -2.062  -25.446 13.674  1.00 55.94  ? 42  MET   A CA   1 
ATOM   322  C  C    . MET   A 1 42  ? -0.685  -25.010 14.198  1.00 52.39  ? 42  MET   A C    1 
ATOM   323  O  O    . MET   A 1 42  ? 0.254   -25.034 13.432  1.00 52.09  ? 42  MET   A O    1 
ATOM   324  C  CB   . MET   A 1 42  ? -2.164  -26.975 13.546  1.00 54.62  ? 42  MET   A CB   1 
ATOM   325  C  CG   . MET   A 1 42  ? -2.135  -27.705 14.883  1.00 63.15  ? 42  MET   A CG   1 
ATOM   326  S  SD   . MET   A 1 42  ? -0.465  -28.167 15.446  1.00 66.46  ? 42  MET   A SD   1 
ATOM   327  C  CE   . MET   A 1 42  ? -0.000  -29.255 14.102  1.00 60.76  ? 42  MET   A CE   1 
ATOM   328  N  N    . GLN   A 1 43  ? -0.560  -24.636 15.466  1.00 57.74  ? 43  GLN   A N    1 
ATOM   329  C  CA   . GLN   A 1 43  ? 0.750   -24.271 16.067  1.00 60.11  ? 43  GLN   A CA   1 
ATOM   330  C  C    . GLN   A 1 43  ? 1.162   -25.384 17.032  1.00 54.63  ? 43  GLN   A C    1 
ATOM   331  O  O    . GLN   A 1 43  ? 0.564   -25.513 18.119  1.00 64.79  ? 43  GLN   A O    1 
ATOM   332  C  CB   . GLN   A 1 43  ? 0.685   -22.880 16.698  1.00 63.77  ? 43  GLN   A CB   1 
ATOM   333  C  CG   . GLN   A 1 43  ? 0.464   -21.776 15.669  1.00 65.09  ? 43  GLN   A CG   1 
ATOM   334  C  CD   . GLN   A 1 43  ? 0.491   -20.404 16.300  1.00 69.25  ? 43  GLN   A CD   1 
ATOM   335  O  OE1  . GLN   A 1 43  ? 1.195   -20.169 17.284  1.00 80.03  ? 43  GLN   A OE1  1 
ATOM   336  N  NE2  . GLN   A 1 43  ? -0.287  -19.493 15.741  1.00 53.78  ? 43  GLN   A NE2  1 
ATOM   337  N  N    . ASN   A 1 44  ? 2.122   -26.185 16.582  1.00 55.47  ? 44  ASN   A N    1 
ATOM   338  C  CA   . ASN   A 1 44  ? 2.783   -27.282 17.330  1.00 56.35  ? 44  ASN   A CA   1 
ATOM   339  C  C    . ASN   A 1 44  ? 3.256   -26.748 18.699  1.00 58.02  ? 44  ASN   A C    1 
ATOM   340  O  O    . ASN   A 1 44  ? 3.990   -25.721 18.748  1.00 55.74  ? 44  ASN   A O    1 
ATOM   341  C  CB   . ASN   A 1 44  ? 3.871   -27.881 16.437  1.00 54.13  ? 44  ASN   A CB   1 
ATOM   342  C  CG   . ASN   A 1 44  ? 4.659   -28.968 17.123  1.00 64.97  ? 44  ASN   A CG   1 
ATOM   343  O  OD1  . ASN   A 1 44  ? 4.099   -29.831 17.797  1.00 62.41  ? 44  ASN   A OD1  1 
ATOM   344  N  ND2  . ASN   A 1 44  ? 5.969   -28.913 16.969  1.00 75.94  ? 44  ASN   A ND2  1 
ATOM   345  N  N    . GLY   A 1 45  ? 2.738   -27.338 19.780  1.00 53.83  ? 45  GLY   A N    1 
ATOM   346  C  CA   . GLY   A 1 45  ? 3.149   -27.062 21.169  1.00 53.76  ? 45  GLY   A CA   1 
ATOM   347  C  C    . GLY   A 1 45  ? 2.457   -25.868 21.810  1.00 50.87  ? 45  GLY   A C    1 
ATOM   348  O  O    . GLY   A 1 45  ? 2.733   -25.632 23.005  1.00 56.87  ? 45  GLY   A O    1 
ATOM   349  N  N    . LYS   A 1 46  ? 1.608   -25.140 21.074  1.00 50.18  ? 46  LYS   A N    1 
ATOM   350  C  CA   . LYS   A 1 46  ? 0.817   -23.984 21.588  1.00 56.25  ? 46  LYS   A CA   1 
ATOM   351  C  C    . LYS   A 1 46  ? -0.602  -24.413 22.001  1.00 51.23  ? 46  LYS   A C    1 
ATOM   352  O  O    . LYS   A 1 46  ? -1.238  -25.191 21.285  1.00 66.71  ? 46  LYS   A O    1 
ATOM   353  C  CB   . LYS   A 1 46  ? 0.676   -22.868 20.541  1.00 60.26  ? 46  LYS   A CB   1 
ATOM   354  C  CG   . LYS   A 1 46  ? 1.968   -22.200 20.087  1.00 65.30  ? 46  LYS   A CG   1 
ATOM   355  C  CD   . LYS   A 1 46  ? 2.554   -21.227 21.075  1.00 73.36  ? 46  LYS   A CD   1 
ATOM   356  C  CE   . LYS   A 1 46  ? 3.711   -20.436 20.493  1.00 85.19  ? 46  LYS   A CE   1 
ATOM   357  N  NZ   . LYS   A 1 46  ? 4.964   -21.233 20.441  1.00 85.06  ? 46  LYS   A NZ   1 
ATOM   358  N  N    . VAL   A 1 47  ? -1.113  -23.799 23.060  1.00 55.02  ? 47  VAL   A N    1 
ATOM   359  C  CA   . VAL   A 1 47  ? -2.518  -23.900 23.550  1.00 48.12  ? 47  VAL   A CA   1 
ATOM   360  C  C    . VAL   A 1 47  ? -3.448  -23.132 22.603  1.00 52.34  ? 47  VAL   A C    1 
ATOM   361  O  O    . VAL   A 1 47  ? -3.315  -21.887 22.471  1.00 53.71  ? 47  VAL   A O    1 
ATOM   362  C  CB   . VAL   A 1 47  ? -2.617  -23.363 24.986  1.00 47.00  ? 47  VAL   A CB   1 
ATOM   363  C  CG1  . VAL   A 1 47  ? -4.047  -23.440 25.500  1.00 49.85  ? 47  VAL   A CG1  1 
ATOM   364  C  CG2  . VAL   A 1 47  ? -1.652  -24.106 25.927  1.00 45.90  ? 47  VAL   A CG2  1 
ATOM   365  N  N    . GLY   A 1 48  ? -4.382  -23.850 21.981  1.00 48.86  ? 48  GLY   A N    1 
ATOM   366  C  CA   . GLY   A 1 48  ? -5.388  -23.289 21.068  1.00 42.86  ? 48  GLY   A CA   1 
ATOM   367  C  C    . GLY   A 1 48  ? -6.779  -23.336 21.674  1.00 39.70  ? 48  GLY   A C    1 
ATOM   368  O  O    . GLY   A 1 48  ? -6.945  -23.967 22.684  1.00 37.89  ? 48  GLY   A O    1 
ATOM   369  N  N    . THR   A 1 49  ? -7.750  -22.712 21.015  1.00 39.71  ? 49  THR   A N    1 
ATOM   370  C  CA   . THR   A 1 49  ? -9.135  -22.547 21.496  1.00 43.00  ? 49  THR   A CA   1 
ATOM   371  C  C    . THR   A 1 49  ? -10.081 -22.830 20.343  1.00 40.36  ? 49  THR   A C    1 
ATOM   372  O  O    . THR   A 1 49  ? -9.919  -22.156 19.321  1.00 45.17  ? 49  THR   A O    1 
ATOM   373  C  CB   . THR   A 1 49  ? -9.346  -21.131 22.052  1.00 47.73  ? 49  THR   A CB   1 
ATOM   374  O  OG1  . THR   A 1 49  ? -8.575  -20.975 23.248  1.00 54.09  ? 49  THR   A OG1  1 
ATOM   375  C  CG2  . THR   A 1 49  ? -10.784 -20.839 22.393  1.00 47.11  ? 49  THR   A CG2  1 
ATOM   376  N  N    . ALA   A 1 50  ? -11.040 -23.747 20.513  1.00 40.28  ? 50  ALA   A N    1 
ATOM   377  C  CA   . ALA   A 1 50  ? -12.141 -23.974 19.543  1.00 41.99  ? 50  ALA   A CA   1 
ATOM   378  C  C    . ALA   A 1 50  ? -13.480 -23.530 20.143  1.00 44.81  ? 50  ALA   A C    1 
ATOM   379  O  O    . ALA   A 1 50  ? -13.774 -23.926 21.297  1.00 46.79  ? 50  ALA   A O    1 
ATOM   380  C  CB   . ALA   A 1 50  ? -12.192 -25.426 19.161  1.00 44.50  ? 50  ALA   A CB   1 
ATOM   381  N  N    . HIS   A 1 51  ? -14.262 -22.763 19.378  1.00 39.02  ? 51  HIS   A N    1 
ATOM   382  C  CA   . HIS   A 1 51  ? -15.636 -22.321 19.734  1.00 39.68  ? 51  HIS   A CA   1 
ATOM   383  C  C    . HIS   A 1 51  ? -16.568 -22.910 18.681  1.00 42.12  ? 51  HIS   A C    1 
ATOM   384  O  O    . HIS   A 1 51  ? -16.296 -22.707 17.499  1.00 44.35  ? 51  HIS   A O    1 
ATOM   385  C  CB   . HIS   A 1 51  ? -15.774 -20.792 19.756  1.00 38.24  ? 51  HIS   A CB   1 
ATOM   386  C  CG   . HIS   A 1 51  ? -14.953 -20.059 20.768  1.00 49.47  ? 51  HIS   A CG   1 
ATOM   387  N  ND1  . HIS   A 1 51  ? -13.693 -19.505 20.460  1.00 54.48  ? 51  HIS   A ND1  1 
ATOM   388  C  CD2  . HIS   A 1 51  ? -15.214 -19.723 22.061  1.00 52.89  ? 51  HIS   A CD2  1 
ATOM   389  C  CE1  . HIS   A 1 51  ? -13.218 -18.885 21.536  1.00 58.27  ? 51  HIS   A CE1  1 
ATOM   390  N  NE2  . HIS   A 1 51  ? -14.126 -19.009 22.542  1.00 56.89  ? 51  HIS   A NE2  1 
ATOM   391  N  N    . ILE   A 1 52  ? -17.582 -23.665 19.071  1.00 41.72  ? 52  ILE   A N    1 
ATOM   392  C  CA   . ILE   A 1 52  ? -18.547 -24.239 18.097  1.00 40.14  ? 52  ILE   A CA   1 
ATOM   393  C  C    . ILE   A 1 52  ? -19.903 -23.660 18.452  1.00 42.95  ? 52  ILE   A C    1 
ATOM   394  O  O    . ILE   A 1 52  ? -20.144 -23.507 19.661  1.00 46.77  ? 52  ILE   A O    1 
ATOM   395  C  CB   . ILE   A 1 52  ? -18.498 -25.773 18.166  1.00 42.79  ? 52  ILE   A CB   1 
ATOM   396  C  CG1  . ILE   A 1 52  ? -17.145 -26.300 17.676  1.00 47.50  ? 52  ILE   A CG1  1 
ATOM   397  C  CG2  . ILE   A 1 52  ? -19.651 -26.395 17.396  1.00 41.35  ? 52  ILE   A CG2  1 
ATOM   398  C  CD1  . ILE   A 1 52  ? -16.294 -26.939 18.736  1.00 44.21  ? 52  ILE   A CD1  1 
ATOM   399  N  N    . ILE   A 1 53  ? -20.722 -23.271 17.476  1.00 43.80  ? 53  ILE   A N    1 
ATOM   400  C  CA   . ILE   A 1 53  ? -22.095 -22.760 17.780  1.00 48.75  ? 53  ILE   A CA   1 
ATOM   401  C  C    . ILE   A 1 53  ? -23.105 -23.288 16.769  1.00 46.78  ? 53  ILE   A C    1 
ATOM   402  O  O    . ILE   A 1 53  ? -22.742 -23.522 15.620  1.00 43.40  ? 53  ILE   A O    1 
ATOM   403  C  CB   . ILE   A 1 53  ? -22.138 -21.230 17.859  1.00 55.70  ? 53  ILE   A CB   1 
ATOM   404  C  CG1  . ILE   A 1 53  ? -21.696 -20.590 16.550  1.00 63.49  ? 53  ILE   A CG1  1 
ATOM   405  C  CG2  . ILE   A 1 53  ? -21.290 -20.738 19.010  1.00 58.30  ? 53  ILE   A CG2  1 
ATOM   406  C  CD1  . ILE   A 1 53  ? -21.536 -19.092 16.674  1.00 71.15  ? 53  ILE   A CD1  1 
ATOM   407  N  N    . TYR   A 1 54  ? -24.333 -23.506 17.227  1.00 47.26  ? 54  TYR   A N    1 
ATOM   408  C  CA   . TYR   A 1 54  ? -25.487 -23.863 16.370  1.00 47.19  ? 54  TYR   A CA   1 
ATOM   409  C  C    . TYR   A 1 54  ? -26.742 -23.174 16.906  1.00 44.37  ? 54  TYR   A C    1 
ATOM   410  O  O    . TYR   A 1 54  ? -26.959 -23.199 18.130  1.00 45.28  ? 54  TYR   A O    1 
ATOM   411  C  CB   . TYR   A 1 54  ? -25.637 -25.380 16.342  1.00 44.32  ? 54  TYR   A CB   1 
ATOM   412  C  CG   . TYR   A 1 54  ? -26.776 -25.857 15.485  1.00 48.03  ? 54  TYR   A CG   1 
ATOM   413  C  CD1  . TYR   A 1 54  ? -26.639 -25.937 14.107  1.00 48.74  ? 54  TYR   A CD1  1 
ATOM   414  C  CD2  . TYR   A 1 54  ? -27.989 -26.241 16.041  1.00 47.96  ? 54  TYR   A CD2  1 
ATOM   415  C  CE1  . TYR   A 1 54  ? -27.683 -26.375 13.300  1.00 49.56  ? 54  TYR   A CE1  1 
ATOM   416  C  CE2  . TYR   A 1 54  ? -29.042 -26.682 15.250  1.00 49.74  ? 54  TYR   A CE2  1 
ATOM   417  C  CZ   . TYR   A 1 54  ? -28.885 -26.747 13.874  1.00 50.26  ? 54  TYR   A CZ   1 
ATOM   418  O  OH   . TYR   A 1 54  ? -29.884 -27.185 13.065  1.00 54.47  ? 54  TYR   A OH   1 
ATOM   419  N  N    . ASN   A 1 55  ? -27.582 -22.615 16.040  1.00 44.33  ? 55  ASN   A N    1 
ATOM   420  C  CA   . ASN   A 1 55  ? -28.988 -22.363 16.458  1.00 48.90  ? 55  ASN   A CA   1 
ATOM   421  C  C    . ASN   A 1 55  ? -29.937 -22.868 15.370  1.00 43.11  ? 55  ASN   A C    1 
ATOM   422  O  O    . ASN   A 1 55  ? -29.531 -22.952 14.215  1.00 43.12  ? 55  ASN   A O    1 
ATOM   423  C  CB   . ASN   A 1 55  ? -29.220 -20.904 16.852  1.00 51.46  ? 55  ASN   A CB   1 
ATOM   424  C  CG   . ASN   A 1 55  ? -29.398 -20.038 15.627  1.00 58.27  ? 55  ASN   A CG   1 
ATOM   425  O  OD1  . ASN   A 1 55  ? -30.332 -20.238 14.856  1.00 66.17  ? 55  ASN   A OD1  1 
ATOM   426  N  ND2  . ASN   A 1 55  ? -28.496 -19.097 15.421  1.00 60.33  ? 55  ASN   A ND2  1 
ATOM   427  N  N    . SER   A 1 56  ? -31.172 -23.155 15.769  1.00 51.24  ? 56  SER   A N    1 
ATOM   428  C  CA   . SER   A 1 56  ? -32.270 -23.749 14.957  1.00 53.06  ? 56  SER   A CA   1 
ATOM   429  C  C    . SER   A 1 56  ? -32.934 -22.674 14.099  1.00 51.47  ? 56  SER   A C    1 
ATOM   430  O  O    . SER   A 1 56  ? -33.730 -23.068 13.226  1.00 61.10  ? 56  SER   A O    1 
ATOM   431  C  CB   . SER   A 1 56  ? -33.298 -24.447 15.830  1.00 46.99  ? 56  SER   A CB   1 
ATOM   432  O  OG   . SER   A 1 56  ? -33.753 -23.567 16.849  1.00 54.35  ? 56  SER   A OG   1 
ATOM   433  N  N    . VAL   A 1 57  ? -32.622 -21.389 14.325  1.00 51.82  ? 57  VAL   A N    1 
ATOM   434  C  CA   . VAL   A 1 57  ? -33.177 -20.270 13.508  1.00 54.64  ? 57  VAL   A CA   1 
ATOM   435  C  C    . VAL   A 1 57  ? -32.322 -20.157 12.242  1.00 56.27  ? 57  VAL   A C    1 
ATOM   436  O  O    . VAL   A 1 57  ? -32.897 -20.277 11.156  1.00 61.27  ? 57  VAL   A O    1 
ATOM   437  C  CB   . VAL   A 1 57  ? -33.278 -18.942 14.286  1.00 56.50  ? 57  VAL   A CB   1 
ATOM   438  C  CG1  . VAL   A 1 57  ? -34.122 -17.914 13.536  1.00 50.49  ? 57  VAL   A CG1  1 
ATOM   439  C  CG2  . VAL   A 1 57  ? -33.845 -19.149 15.692  1.00 56.25  ? 57  VAL   A CG2  1 
ATOM   440  N  N    . ASP   A 1 58  ? -31.005 -19.990 12.386  1.00 60.24  ? 58  ASP   A N    1 
ATOM   441  C  CA   . ASP   A 1 58  ? -30.012 -19.955 11.274  1.00 61.70  ? 58  ASP   A CA   1 
ATOM   442  C  C    . ASP   A 1 58  ? -29.822 -21.334 10.652  1.00 59.93  ? 58  ASP   A C    1 
ATOM   443  O  O    . ASP   A 1 58  ? -29.455 -21.362 9.489   1.00 55.48  ? 58  ASP   A O    1 
ATOM   444  C  CB   . ASP   A 1 58  ? -28.601 -19.591 11.733  1.00 69.34  ? 58  ASP   A CB   1 
ATOM   445  C  CG   . ASP   A 1 58  ? -28.485 -18.207 12.329  1.00 75.53  ? 58  ASP   A CG   1 
ATOM   446  O  OD1  . ASP   A 1 58  ? -29.477 -17.438 12.198  1.00 65.57  ? 58  ASP   A OD1  1 
ATOM   447  O  OD2  . ASP   A 1 58  ? -27.390 -17.913 12.905  1.00 81.98  ? 58  ASP   A OD2  1 
ATOM   448  N  N    . LYS   A 1 59  ? -29.969 -22.422 11.425  1.00 60.06  ? 59  LYS   A N    1 
ATOM   449  C  CA   . LYS   A 1 59  ? -29.638 -23.807 10.981  1.00 60.35  ? 59  LYS   A CA   1 
ATOM   450  C  C    . LYS   A 1 59  ? -28.216 -23.816 10.384  1.00 55.17  ? 59  LYS   A C    1 
ATOM   451  O  O    . LYS   A 1 59  ? -27.993 -24.506 9.399   1.00 61.29  ? 59  LYS   A O    1 
ATOM   452  C  CB   . LYS   A 1 59  ? -30.697 -24.323 10.000  1.00 58.52  ? 59  LYS   A CB   1 
ATOM   453  C  CG   . LYS   A 1 59  ? -32.023 -24.743 10.627  1.00 66.76  ? 59  LYS   A CG   1 
ATOM   454  C  CD   . LYS   A 1 59  ? -33.197 -24.814 9.651   1.00 77.17  ? 59  LYS   A CD   1 
ATOM   455  C  CE   . LYS   A 1 59  ? -34.564 -24.758 10.308  1.00 84.35  ? 59  LYS   A CE   1 
ATOM   456  N  NZ   . LYS   A 1 59  ? -34.726 -25.821 11.327  1.00 91.58  ? 59  LYS   A NZ   1 
ATOM   457  N  N    . ARG   A 1 60  ? -27.290 -23.077 10.993  1.00 50.47  ? 60  ARG   A N    1 
ATOM   458  C  CA   . ARG   A 1 60  ? -25.881 -22.943 10.564  1.00 54.06  ? 60  ARG   A CA   1 
ATOM   459  C  C    . ARG   A 1 60  ? -24.981 -23.470 11.688  1.00 58.39  ? 60  ARG   A C    1 
ATOM   460  O  O    . ARG   A 1 60  ? -25.085 -22.940 12.808  1.00 52.40  ? 60  ARG   A O    1 
ATOM   461  C  CB   . ARG   A 1 60  ? -25.551 -21.481 10.260  1.00 60.30  ? 60  ARG   A CB   1 
ATOM   462  C  CG   . ARG   A 1 60  ? -24.531 -21.329 9.142   1.00 77.23  ? 60  ARG   A CG   1 
ATOM   463  C  CD   . ARG   A 1 60  ? -24.123 -19.895 8.880   1.00 90.18  ? 60  ARG   A CD   1 
ATOM   464  N  NE   . ARG   A 1 60  ? -25.133 -19.166 8.130   1.00 100.96 ? 60  ARG   A NE   1 
ATOM   465  C  CZ   . ARG   A 1 60  ? -25.184 -19.078 6.809   1.00 108.18 ? 60  ARG   A CZ   1 
ATOM   466  N  NH1  . ARG   A 1 60  ? -26.149 -18.376 6.239   1.00 105.30 ? 60  ARG   A NH1  1 
ATOM   467  N  NH2  . ARG   A 1 60  ? -24.277 -19.686 6.063   1.00 115.84 ? 60  ARG   A NH2  1 
ATOM   468  N  N    . LEU   A 1 61  ? -24.160 -24.494 11.410  1.00 55.28  ? 61  LEU   A N    1 
ATOM   469  C  CA   . LEU   A 1 61  ? -23.163 -25.039 12.370  1.00 47.96  ? 61  LEU   A CA   1 
ATOM   470  C  C    . LEU   A 1 61  ? -21.820 -24.406 12.037  1.00 47.51  ? 61  LEU   A C    1 
ATOM   471  O  O    . LEU   A 1 61  ? -21.333 -24.635 10.906  1.00 48.58  ? 61  LEU   A O    1 
ATOM   472  C  CB   . LEU   A 1 61  ? -23.100 -26.565 12.278  1.00 45.60  ? 61  LEU   A CB   1 
ATOM   473  C  CG   . LEU   A 1 61  ? -21.963 -27.209 13.064  1.00 47.86  ? 61  LEU   A CG   1 
ATOM   474  C  CD1  . LEU   A 1 61  ? -22.176 -27.016 14.554  1.00 47.02  ? 61  LEU   A CD1  1 
ATOM   475  C  CD2  . LEU   A 1 61  ? -21.842 -28.698 12.740  1.00 50.14  ? 61  LEU   A CD2  1 
ATOM   476  N  N    . SER   A 1 62  ? -21.273 -23.631 12.969  1.00 40.74  ? 62  SER   A N    1 
ATOM   477  C  CA   . SER   A 1 62  ? -20.040 -22.849 12.762  1.00 48.16  ? 62  SER   A CA   1 
ATOM   478  C  C    . SER   A 1 62  ? -19.001 -23.209 13.813  1.00 51.11  ? 62  SER   A C    1 
ATOM   479  O  O    . SER   A 1 62  ? -19.384 -23.600 14.935  1.00 48.71  ? 62  SER   A O    1 
ATOM   480  C  CB   . SER   A 1 62  ? -20.348 -21.401 12.766  1.00 56.03  ? 62  SER   A CB   1 
ATOM   481  O  OG   . SER   A 1 62  ? -21.408 -21.150 11.852  1.00 69.56  ? 62  SER   A OG   1 
ATOM   482  N  N    . ALA   A 1 63  ? -17.729 -23.105 13.427  1.00 47.96  ? 63  ALA   A N    1 
ATOM   483  C  CA   . ALA   A 1 63  ? -16.566 -23.335 14.307  1.00 46.69  ? 63  ALA   A CA   1 
ATOM   484  C  C    . ALA   A 1 63  ? -15.518 -22.277 13.996  1.00 46.48  ? 63  ALA   A C    1 
ATOM   485  O  O    . ALA   A 1 63  ? -15.347 -21.918 12.807  1.00 49.41  ? 63  ALA   A O    1 
ATOM   486  C  CB   . ALA   A 1 63  ? -16.004 -24.720 14.136  1.00 46.44  ? 63  ALA   A CB   1 
ATOM   487  N  N    . VAL   A 1 64  ? -14.851 -21.825 15.046  1.00 44.08  ? 64  VAL   A N    1 
ATOM   488  C  CA   . VAL   A 1 64  ? -13.735 -20.853 14.998  1.00 44.65  ? 64  VAL   A CA   1 
ATOM   489  C  C    . VAL   A 1 64  ? -12.629 -21.451 15.840  1.00 40.16  ? 64  VAL   A C    1 
ATOM   490  O  O    . VAL   A 1 64  ? -12.899 -21.776 16.994  1.00 42.44  ? 64  VAL   A O    1 
ATOM   491  C  CB   . VAL   A 1 64  ? -14.098 -19.469 15.571  1.00 52.17  ? 64  VAL   A CB   1 
ATOM   492  C  CG1  . VAL   A 1 64  ? -12.970 -18.478 15.337  1.00 52.84  ? 64  VAL   A CG1  1 
ATOM   493  C  CG2  . VAL   A 1 64  ? -15.380 -18.920 15.004  1.00 60.08  ? 64  VAL   A CG2  1 
ATOM   494  N  N    . VAL   A 1 65  ? -11.424 -21.499 15.295  1.00 41.76  ? 65  VAL   A N    1 
ATOM   495  C  CA   . VAL   A 1 65  ? -10.222 -21.995 16.022  1.00 41.17  ? 65  VAL   A CA   1 
ATOM   496  C  C    . VAL   A 1 65  ? -9.159  -20.906 15.919  1.00 40.11  ? 65  VAL   A C    1 
ATOM   497  O  O    . VAL   A 1 65  ? -8.920  -20.375 14.826  1.00 46.63  ? 65  VAL   A O    1 
ATOM   498  C  CB   . VAL   A 1 65  ? -9.738  -23.344 15.467  1.00 45.46  ? 65  VAL   A CB   1 
ATOM   499  C  CG1  . VAL   A 1 65  ? -8.599  -23.906 16.304  1.00 45.78  ? 65  VAL   A CG1  1 
ATOM   500  C  CG2  . VAL   A 1 65  ? -10.891 -24.346 15.383  1.00 53.50  ? 65  VAL   A CG2  1 
ATOM   501  N  N    . SER   A 1 66  ? -8.553  -20.584 17.038  1.00 40.80  ? 66  SER   A N    1 
ATOM   502  C  CA   . SER   A 1 66  ? -7.646  -19.433 17.170  1.00 43.62  ? 66  SER   A CA   1 
ATOM   503  C  C    . SER   A 1 66  ? -6.538  -19.827 18.130  1.00 46.18  ? 66  SER   A C    1 
ATOM   504  O  O    . SER   A 1 66  ? -6.722  -20.785 18.910  1.00 47.78  ? 66  SER   A O    1 
ATOM   505  C  CB   . SER   A 1 66  ? -8.428  -18.220 17.614  1.00 54.48  ? 66  SER   A CB   1 
ATOM   506  O  OG   . SER   A 1 66  ? -9.089  -18.425 18.854  1.00 51.43  ? 66  SER   A OG   1 
ATOM   507  N  N    . TYR   A 1 67  ? -5.412  -19.149 18.024  1.00 54.08  ? 67  TYR   A N    1 
ATOM   508  C  CA   . TYR   A 1 67  ? -4.279  -19.207 18.983  1.00 51.89  ? 67  TYR   A CA   1 
ATOM   509  C  C    . TYR   A 1 67  ? -3.995  -17.775 19.431  1.00 49.49  ? 67  TYR   A C    1 
ATOM   510  O  O    . TYR   A 1 67  ? -4.288  -16.859 18.668  1.00 46.24  ? 67  TYR   A O    1 
ATOM   511  C  CB   . TYR   A 1 67  ? -3.086  -19.786 18.236  1.00 49.42  ? 67  TYR   A CB   1 
ATOM   512  C  CG   . TYR   A 1 67  ? -3.087  -21.273 18.016  1.00 50.17  ? 67  TYR   A CG   1 
ATOM   513  C  CD1  . TYR   A 1 67  ? -2.583  -22.122 18.991  1.00 52.17  ? 67  TYR   A CD1  1 
ATOM   514  C  CD2  . TYR   A 1 67  ? -3.499  -21.832 16.811  1.00 50.45  ? 67  TYR   A CD2  1 
ATOM   515  C  CE1  . TYR   A 1 67  ? -2.522  -23.493 18.799  1.00 50.73  ? 67  TYR   A CE1  1 
ATOM   516  C  CE2  . TYR   A 1 67  ? -3.444  -23.207 16.604  1.00 54.87  ? 67  TYR   A CE2  1 
ATOM   517  C  CZ   . TYR   A 1 67  ? -2.941  -24.045 17.600  1.00 57.65  ? 67  TYR   A CZ   1 
ATOM   518  O  OH   . TYR   A 1 67  ? -2.824  -25.409 17.432  1.00 56.76  ? 67  TYR   A OH   1 
ATOM   519  N  N    . PRO   A 1 68  ? -3.389  -17.484 20.604  1.00 56.69  ? 68  PRO   A N    1 
ATOM   520  C  CA   . PRO   A 1 68  ? -2.978  -16.099 20.892  1.00 62.44  ? 68  PRO   A CA   1 
ATOM   521  C  C    . PRO   A 1 68  ? -2.126  -15.496 19.755  1.00 58.86  ? 68  PRO   A C    1 
ATOM   522  O  O    . PRO   A 1 68  ? -1.172  -16.121 19.319  1.00 65.14  ? 68  PRO   A O    1 
ATOM   523  C  CB   . PRO   A 1 68  ? -2.201  -16.194 22.219  1.00 58.96  ? 68  PRO   A CB   1 
ATOM   524  C  CG   . PRO   A 1 68  ? -2.720  -17.476 22.871  1.00 61.51  ? 68  PRO   A CG   1 
ATOM   525  C  CD   . PRO   A 1 68  ? -3.108  -18.400 21.720  1.00 60.55  ? 68  PRO   A CD   1 
ATOM   526  N  N    . ASN   A 1 69  ? -2.543  -14.329 19.264  1.00 66.19  ? 69  ASN   A N    1 
ATOM   527  C  CA   . ASN   A 1 69  ? -1.775  -13.413 18.374  1.00 72.16  ? 69  ASN   A CA   1 
ATOM   528  C  C    . ASN   A 1 69  ? -1.739  -13.952 16.949  1.00 73.85  ? 69  ASN   A C    1 
ATOM   529  O  O    . ASN   A 1 69  ? -0.773  -13.628 16.251  1.00 73.94  ? 69  ASN   A O    1 
ATOM   530  C  CB   . ASN   A 1 69  ? -0.353  -13.163 18.891  1.00 69.56  ? 69  ASN   A CB   1 
ATOM   531  C  CG   . ASN   A 1 69  ? -0.367  -12.581 20.287  1.00 79.62  ? 69  ASN   A CG   1 
ATOM   532  O  OD1  . ASN   A 1 69  ? 0.310   -13.089 21.187  1.00 76.92  ? 69  ASN   A OD1  1 
ATOM   533  N  ND2  . ASN   A 1 69  ? -1.187  -11.554 20.481  1.00 70.14  ? 69  ASN   A ND2  1 
ATOM   534  N  N    . ALA   A 1 70  ? -2.751  -14.710 16.517  1.00 74.55  ? 70  ALA   A N    1 
ATOM   535  C  CA   . ALA   A 1 70  ? -2.811  -15.248 15.136  1.00 70.73  ? 70  ALA   A CA   1 
ATOM   536  C  C    . ALA   A 1 70  ? -4.182  -14.981 14.545  1.00 60.89  ? 70  ALA   A C    1 
ATOM   537  O  O    . ALA   A 1 70  ? -5.119  -14.835 15.319  1.00 60.44  ? 70  ALA   A O    1 
ATOM   538  C  CB   . ALA   A 1 70  ? -2.489  -16.721 15.104  1.00 64.55  ? 70  ALA   A CB   1 
ATOM   539  N  N    . ASP   A 1 71  ? -4.248  -14.913 13.218  1.00 66.47  ? 71  ASP   A N    1 
ATOM   540  C  CA   . ASP   A 1 71  ? -5.501  -15.063 12.438  1.00 68.68  ? 71  ASP   A CA   1 
ATOM   541  C  C    . ASP   A 1 71  ? -6.228  -16.335 12.908  1.00 72.10  ? 71  ASP   A C    1 
ATOM   542  O  O    . ASP   A 1 71  ? -5.562  -17.347 13.265  1.00 72.60  ? 71  ASP   A O    1 
ATOM   543  C  CB   . ASP   A 1 71  ? -5.219  -15.125 10.934  1.00 77.27  ? 71  ASP   A CB   1 
ATOM   544  C  CG   . ASP   A 1 71  ? -5.275  -13.777 10.239  1.00 90.98  ? 71  ASP   A CG   1 
ATOM   545  O  OD1  . ASP   A 1 71  ? -6.385  -13.222 10.133  1.00 91.35  ? 71  ASP   A OD1  1 
ATOM   546  O  OD2  . ASP   A 1 71  ? -4.209  -13.295 9.803   1.00 97.02  ? 71  ASP   A OD2  1 
ATOM   547  N  N    . SER   A 1 72  ? -7.554  -16.270 12.908  1.00 61.77  ? 72  SER   A N    1 
ATOM   548  C  CA   . SER   A 1 72  ? -8.474  -17.400 13.167  1.00 61.54  ? 72  SER   A CA   1 
ATOM   549  C  C    . SER   A 1 72  ? -8.697  -18.181 11.873  1.00 56.40  ? 72  SER   A C    1 
ATOM   550  O  O    . SER   A 1 72  ? -8.448  -17.625 10.788  1.00 55.73  ? 72  SER   A O    1 
ATOM   551  C  CB   . SER   A 1 72  ? -9.787  -16.891 13.718  1.00 55.60  ? 72  SER   A CB   1 
ATOM   552  O  OG   . SER   A 1 72  ? -9.581  -16.342 15.008  1.00 64.37  ? 72  SER   A OG   1 
ATOM   553  N  N    . ALA   A 1 73  ? -9.201  -19.403 12.008  1.00 46.69  ? 73  ALA   A N    1 
ATOM   554  C  CA   . ALA   A 1 73  ? -9.832  -20.195 10.929  1.00 47.86  ? 73  ALA   A CA   1 
ATOM   555  C  C    . ALA   A 1 73  ? -11.270 -20.465 11.348  1.00 44.37  ? 73  ALA   A C    1 
ATOM   556  O  O    . ALA   A 1 73  ? -11.473 -20.815 12.520  1.00 48.40  ? 73  ALA   A O    1 
ATOM   557  C  CB   . ALA   A 1 73  ? -9.085  -21.492 10.705  1.00 44.16  ? 73  ALA   A CB   1 
ATOM   558  N  N    . THR   A 1 74  ? -12.214 -20.285 10.437  1.00 42.02  ? 74  THR   A N    1 
ATOM   559  C  CA   . THR   A 1 74  ? -13.651 -20.469 10.702  1.00 47.32  ? 74  THR   A CA   1 
ATOM   560  C  C    . THR   A 1 74  ? -14.246 -21.286 9.557   1.00 44.22  ? 74  THR   A C    1 
ATOM   561  O  O    . THR   A 1 74  ? -13.767 -21.223 8.426   1.00 45.37  ? 74  THR   A O    1 
ATOM   562  C  CB   . THR   A 1 74  ? -14.377 -19.135 10.980  1.00 52.90  ? 74  THR   A CB   1 
ATOM   563  O  OG1  . THR   A 1 74  ? -14.952 -18.681 9.762   1.00 57.74  ? 74  THR   A OG1  1 
ATOM   564  C  CG2  . THR   A 1 74  ? -13.497 -18.044 11.548  1.00 54.58  ? 74  THR   A CG2  1 
ATOM   565  N  N    . VAL   A 1 75  ? -15.273 -22.052 9.862   1.00 47.73  ? 75  VAL   A N    1 
ATOM   566  C  CA   . VAL   A 1 75  ? -15.955 -22.887 8.848   1.00 42.01  ? 75  VAL   A CA   1 
ATOM   567  C  C    . VAL   A 1 75  ? -17.404 -22.969 9.302   1.00 43.89  ? 75  VAL   A C    1 
ATOM   568  O  O    . VAL   A 1 75  ? -17.648 -22.920 10.519  1.00 51.70  ? 75  VAL   A O    1 
ATOM   569  C  CB   . VAL   A 1 75  ? -15.204 -24.225 8.720   1.00 48.80  ? 75  VAL   A CB   1 
ATOM   570  C  CG1  . VAL   A 1 75  ? -15.325 -25.121 9.951   1.00 48.89  ? 75  VAL   A CG1  1 
ATOM   571  C  CG2  . VAL   A 1 75  ? -15.567 -24.970 7.459   1.00 51.69  ? 75  VAL   A CG2  1 
ATOM   572  N  N    . SER   A 1 76  ? -18.313 -22.942 8.342   1.00 49.18  ? 76  SER   A N    1 
ATOM   573  C  CA   . SER   A 1 76  ? -19.781 -22.839 8.504   1.00 52.15  ? 76  SER   A CA   1 
ATOM   574  C  C    . SER   A 1 76  ? -20.430 -23.736 7.470   1.00 57.05  ? 76  SER   A C    1 
ATOM   575  O  O    . SER   A 1 76  ? -20.019 -23.690 6.291   1.00 64.47  ? 76  SER   A O    1 
ATOM   576  C  CB   . SER   A 1 76  ? -20.266 -21.439 8.322   1.00 53.32  ? 76  SER   A CB   1 
ATOM   577  O  OG   . SER   A 1 76  ? -19.998 -20.687 9.486   1.00 61.71  ? 76  SER   A OG   1 
ATOM   578  N  N    . TYR   A 1 77  ? -21.409 -24.515 7.898   1.00 56.65  ? 77  TYR   A N    1 
ATOM   579  C  CA   . TYR   A 1 77  ? -22.215 -25.328 6.973   1.00 56.59  ? 77  TYR   A CA   1 
ATOM   580  C  C    . TYR   A 1 77  ? -23.667 -25.226 7.418   1.00 58.86  ? 77  TYR   A C    1 
ATOM   581  O  O    . TYR   A 1 77  ? -23.914 -25.406 8.621   1.00 59.75  ? 77  TYR   A O    1 
ATOM   582  C  CB   . TYR   A 1 77  ? -21.656 -26.740 6.944   1.00 51.17  ? 77  TYR   A CB   1 
ATOM   583  C  CG   . TYR   A 1 77  ? -22.335 -27.633 5.947   1.00 52.43  ? 77  TYR   A CG   1 
ATOM   584  C  CD1  . TYR   A 1 77  ? -22.243 -27.409 4.570   1.00 48.72  ? 77  TYR   A CD1  1 
ATOM   585  C  CD2  . TYR   A 1 77  ? -23.011 -28.756 6.393   1.00 51.68  ? 77  TYR   A CD2  1 
ATOM   586  C  CE1  . TYR   A 1 77  ? -22.849 -28.270 3.668   1.00 44.90  ? 77  TYR   A CE1  1 
ATOM   587  C  CE2  . TYR   A 1 77  ? -23.599 -29.638 5.503   1.00 52.36  ? 77  TYR   A CE2  1 
ATOM   588  C  CZ   . TYR   A 1 77  ? -23.535 -29.381 4.146   1.00 49.07  ? 77  TYR   A CZ   1 
ATOM   589  O  OH   . TYR   A 1 77  ? -24.158 -30.285 3.346   1.00 59.62  ? 77  TYR   A OH   1 
ATOM   590  N  N    . ASP   A 1 78  ? -24.540 -24.859 6.476   1.00 59.13  ? 78  ASP   A N    1 
ATOM   591  C  CA   . ASP   A 1 78  ? -26.016 -24.890 6.596   1.00 57.42  ? 78  ASP   A CA   1 
ATOM   592  C  C    . ASP   A 1 78  ? -26.450 -26.340 6.711   1.00 56.95  ? 78  ASP   A C    1 
ATOM   593  O  O    . ASP   A 1 78  ? -26.283 -27.122 5.751   1.00 55.85  ? 78  ASP   A O    1 
ATOM   594  C  CB   . ASP   A 1 78  ? -26.736 -24.269 5.399   1.00 64.26  ? 78  ASP   A CB   1 
ATOM   595  C  CG   . ASP   A 1 78  ? -27.020 -22.805 5.618   1.00 71.87  ? 78  ASP   A CG   1 
ATOM   596  O  OD1  . ASP   A 1 78  ? -28.090 -22.495 6.215   1.00 81.70  ? 78  ASP   A OD1  1 
ATOM   597  O  OD2  . ASP   A 1 78  ? -26.150 -22.001 5.255   1.00 72.36  ? 78  ASP   A OD2  1 
ATOM   598  N  N    . VAL   A 1 79  ? -27.010 -26.679 7.855   1.00 56.76  ? 79  VAL   A N    1 
ATOM   599  C  CA   . VAL   A 1 79  ? -27.520 -28.047 8.085   1.00 55.25  ? 79  VAL   A CA   1 
ATOM   600  C  C    . VAL   A 1 79  ? -28.592 -27.938 9.153   1.00 52.34  ? 79  VAL   A C    1 
ATOM   601  O  O    . VAL   A 1 79  ? -28.441 -27.134 10.092  1.00 51.89  ? 79  VAL   A O    1 
ATOM   602  C  CB   . VAL   A 1 79  ? -26.379 -29.022 8.450   1.00 56.00  ? 79  VAL   A CB   1 
ATOM   603  C  CG1  . VAL   A 1 79  ? -25.566 -28.552 9.659   1.00 53.32  ? 79  VAL   A CG1  1 
ATOM   604  C  CG2  . VAL   A 1 79  ? -26.910 -30.435 8.660   1.00 54.93  ? 79  VAL   A CG2  1 
ATOM   605  N  N    . ASP   A 1 80  ? -29.650 -28.703 8.952   1.00 59.69  ? 80  ASP   A N    1 
ATOM   606  C  CA   . ASP   A 1 80  ? -30.806 -28.803 9.866   1.00 59.09  ? 80  ASP   A CA   1 
ATOM   607  C  C    . ASP   A 1 80  ? -30.567 -30.038 10.726  1.00 56.15  ? 80  ASP   A C    1 
ATOM   608  O  O    . ASP   A 1 80  ? -30.879 -31.151 10.249  1.00 58.97  ? 80  ASP   A O    1 
ATOM   609  C  CB   . ASP   A 1 80  ? -32.108 -28.925 9.068   1.00 58.95  ? 80  ASP   A CB   1 
ATOM   610  C  CG   . ASP   A 1 80  ? -33.329 -28.957 9.969   1.00 71.92  ? 80  ASP   A CG   1 
ATOM   611  O  OD1  . ASP   A 1 80  ? -33.155 -29.161 11.213  1.00 66.96  ? 80  ASP   A OD1  1 
ATOM   612  O  OD2  . ASP   A 1 80  ? -34.438 -28.722 9.441   1.00 77.35  ? 80  ASP   A OD2  1 
ATOM   613  N  N    . LEU   A 1 81  ? -30.036 -29.870 11.934  1.00 57.82  ? 81  LEU   A N    1 
ATOM   614  C  CA   . LEU   A 1 81  ? -29.610 -31.028 12.774  1.00 56.32  ? 81  LEU   A CA   1 
ATOM   615  C  C    . LEU   A 1 81  ? -30.831 -31.799 13.327  1.00 59.00  ? 81  LEU   A C    1 
ATOM   616  O  O    . LEU   A 1 81  ? -30.645 -32.971 13.698  1.00 58.20  ? 81  LEU   A O    1 
ATOM   617  C  CB   . LEU   A 1 81  ? -28.654 -30.521 13.859  1.00 60.72  ? 81  LEU   A CB   1 
ATOM   618  C  CG   . LEU   A 1 81  ? -27.340 -29.904 13.352  1.00 58.07  ? 81  LEU   A CG   1 
ATOM   619  C  CD1  . LEU   A 1 81  ? -26.410 -29.539 14.506  1.00 59.83  ? 81  LEU   A CD1  1 
ATOM   620  C  CD2  . LEU   A 1 81  ? -26.610 -30.832 12.401  1.00 55.21  ? 81  LEU   A CD2  1 
ATOM   621  N  N    . ASP   A 1 82  ? -32.048 -31.230 13.286  1.00 61.81  ? 82  ASP   A N    1 
ATOM   622  C  CA   . ASP   A 1 82  ? -33.321 -31.943 13.608  1.00 62.70  ? 82  ASP   A CA   1 
ATOM   623  C  C    . ASP   A 1 82  ? -33.536 -33.115 12.633  1.00 61.86  ? 82  ASP   A C    1 
ATOM   624  O  O    . ASP   A 1 82  ? -34.301 -34.037 12.990  1.00 63.67  ? 82  ASP   A O    1 
ATOM   625  C  CB   . ASP   A 1 82  ? -34.571 -31.050 13.541  1.00 74.11  ? 82  ASP   A CB   1 
ATOM   626  C  CG   . ASP   A 1 82  ? -34.506 -29.632 14.125  1.00 86.72  ? 82  ASP   A CG   1 
ATOM   627  O  OD1  . ASP   A 1 82  ? -33.588 -29.318 14.949  1.00 88.81  ? 82  ASP   A OD1  1 
ATOM   628  O  OD2  . ASP   A 1 82  ? -35.391 -28.828 13.746  1.00 84.86  ? 82  ASP   A OD2  1 
ATOM   629  N  N    . ASN   A 1 83  ? -32.882 -33.082 11.464  1.00 59.83  ? 83  ASN   A N    1 
ATOM   630  C  CA   . ASN   A 1 83  ? -32.996 -34.077 10.360  1.00 60.02  ? 83  ASN   A CA   1 
ATOM   631  C  C    . ASN   A 1 83  ? -31.833 -35.056 10.309  1.00 58.12  ? 83  ASN   A C    1 
ATOM   632  O  O    . ASN   A 1 83  ? -31.844 -35.873 9.387   1.00 67.22  ? 83  ASN   A O    1 
ATOM   633  C  CB   . ASN   A 1 83  ? -32.948 -33.433 8.973   1.00 61.08  ? 83  ASN   A CB   1 
ATOM   634  C  CG   . ASN   A 1 83  ? -34.186 -32.607 8.718   1.00 71.72  ? 83  ASN   A CG   1 
ATOM   635  O  OD1  . ASN   A 1 83  ? -35.240 -32.894 9.286   1.00 70.44  ? 83  ASN   A OD1  1 
ATOM   636  N  ND2  . ASN   A 1 83  ? -34.048 -31.558 7.922   1.00 73.56  ? 83  ASN   A ND2  1 
ATOM   637  N  N    . VAL   A 1 84  ? -30.844 -34.943 11.194  1.00 57.35  ? 84  VAL   A N    1 
ATOM   638  C  CA   . VAL   A 1 84  ? -29.600 -35.764 11.126  1.00 53.72  ? 84  VAL   A CA   1 
ATOM   639  C  C    . VAL   A 1 84  ? -29.411 -36.509 12.445  1.00 51.75  ? 84  VAL   A C    1 
ATOM   640  O  O    . VAL   A 1 84  ? -29.002 -37.666 12.397  1.00 64.17  ? 84  VAL   A O    1 
ATOM   641  C  CB   . VAL   A 1 84  ? -28.379 -34.879 10.814  1.00 59.94  ? 84  VAL   A CB   1 
ATOM   642  C  CG1  . VAL   A 1 84  ? -27.097 -35.684 10.802  1.00 57.37  ? 84  VAL   A CG1  1 
ATOM   643  C  CG2  . VAL   A 1 84  ? -28.538 -34.105 9.511   1.00 61.63  ? 84  VAL   A CG2  1 
ATOM   644  N  N    . LEU   A 1 85  ? -29.603 -35.833 13.578  1.00 56.23  ? 85  LEU   A N    1 
ATOM   645  C  CA   . LEU   A 1 85  ? -29.346 -36.383 14.932  1.00 53.33  ? 85  LEU   A CA   1 
ATOM   646  C  C    . LEU   A 1 85  ? -30.653 -36.915 15.509  1.00 51.64  ? 85  LEU   A C    1 
ATOM   647  O  O    . LEU   A 1 85  ? -31.731 -36.413 15.193  1.00 51.99  ? 85  LEU   A O    1 
ATOM   648  C  CB   . LEU   A 1 85  ? -28.772 -35.264 15.802  1.00 51.87  ? 85  LEU   A CB   1 
ATOM   649  C  CG   . LEU   A 1 85  ? -27.385 -34.761 15.396  1.00 55.17  ? 85  LEU   A CG   1 
ATOM   650  C  CD1  . LEU   A 1 85  ? -27.022 -33.482 16.130  1.00 55.66  ? 85  LEU   A CD1  1 
ATOM   651  C  CD2  . LEU   A 1 85  ? -26.335 -35.817 15.661  1.00 55.65  ? 85  LEU   A CD2  1 
ATOM   652  N  N    . PRO   A 1 86  ? -30.608 -37.909 16.413  1.00 47.82  ? 86  PRO   A N    1 
ATOM   653  C  CA   . PRO   A 1 86  ? -31.765 -38.187 17.258  1.00 45.75  ? 86  PRO   A CA   1 
ATOM   654  C  C    . PRO   A 1 86  ? -32.018 -36.969 18.180  1.00 51.54  ? 86  PRO   A C    1 
ATOM   655  O  O    . PRO   A 1 86  ? -31.220 -36.021 18.187  1.00 45.79  ? 86  PRO   A O    1 
ATOM   656  C  CB   . PRO   A 1 86  ? -31.407 -39.476 18.000  1.00 43.76  ? 86  PRO   A CB   1 
ATOM   657  C  CG   . PRO   A 1 86  ? -29.908 -39.660 17.844  1.00 51.64  ? 86  PRO   A CG   1 
ATOM   658  C  CD   . PRO   A 1 86  ? -29.441 -38.748 16.720  1.00 51.51  ? 86  PRO   A CD   1 
ATOM   659  N  N    . GLU   A 1 87  ? -33.159 -36.953 18.876  1.00 50.62  ? 87  GLU   A N    1 
ATOM   660  C  CA   . GLU   A 1 87  ? -33.581 -35.862 19.793  1.00 52.36  ? 87  GLU   A CA   1 
ATOM   661  C  C    . GLU   A 1 87  ? -32.635 -35.818 20.993  1.00 46.69  ? 87  GLU   A C    1 
ATOM   662  O  O    . GLU   A 1 87  ? -32.294 -34.707 21.472  1.00 52.20  ? 87  GLU   A O    1 
ATOM   663  C  CB   . GLU   A 1 87  ? -35.005 -36.112 20.293  1.00 66.40  ? 87  GLU   A CB   1 
ATOM   664  C  CG   . GLU   A 1 87  ? -36.089 -35.474 19.456  1.00 74.27  ? 87  GLU   A CG   1 
ATOM   665  C  CD   . GLU   A 1 87  ? -37.449 -35.469 20.132  1.00 77.66  ? 87  GLU   A CD   1 
ATOM   666  O  OE1  . GLU   A 1 87  ? -37.516 -35.264 21.374  1.00 69.44  ? 87  GLU   A OE1  1 
ATOM   667  O  OE2  . GLU   A 1 87  ? -38.437 -35.649 19.409  1.00 92.93  ? 87  GLU   A OE2  1 
ATOM   668  N  N    . TRP   A 1 88  ? -32.264 -37.000 21.483  1.00 43.08  ? 88  TRP   A N    1 
ATOM   669  C  CA   . TRP   A 1 88  ? -31.343 -37.173 22.628  1.00 43.74  ? 88  TRP   A CA   1 
ATOM   670  C  C    . TRP   A 1 88  ? -30.023 -37.707 22.113  1.00 42.43  ? 88  TRP   A C    1 
ATOM   671  O  O    . TRP   A 1 88  ? -30.026 -38.717 21.418  1.00 45.79  ? 88  TRP   A O    1 
ATOM   672  C  CB   . TRP   A 1 88  ? -31.921 -38.094 23.695  1.00 45.50  ? 88  TRP   A CB   1 
ATOM   673  C  CG   . TRP   A 1 88  ? -33.111 -37.530 24.402  1.00 52.36  ? 88  TRP   A CG   1 
ATOM   674  C  CD1  . TRP   A 1 88  ? -34.431 -37.701 24.082  1.00 48.53  ? 88  TRP   A CD1  1 
ATOM   675  C  CD2  . TRP   A 1 88  ? -33.083 -36.720 25.585  1.00 48.77  ? 88  TRP   A CD2  1 
ATOM   676  N  NE1  . TRP   A 1 88  ? -35.223 -37.040 24.985  1.00 54.01  ? 88  TRP   A NE1  1 
ATOM   677  C  CE2  . TRP   A 1 88  ? -34.426 -36.439 25.925  1.00 50.62  ? 88  TRP   A CE2  1 
ATOM   678  C  CE3  . TRP   A 1 88  ? -32.065 -36.252 26.414  1.00 46.49  ? 88  TRP   A CE3  1 
ATOM   679  C  CZ2  . TRP   A 1 88  ? -34.767 -35.697 27.053  1.00 45.99  ? 88  TRP   A CZ2  1 
ATOM   680  C  CZ3  . TRP   A 1 88  ? -32.404 -35.498 27.520  1.00 46.81  ? 88  TRP   A CZ3  1 
ATOM   681  C  CH2  . TRP   A 1 88  ? -33.736 -35.224 27.832  1.00 48.82  ? 88  TRP   A CH2  1 
ATOM   682  N  N    . VAL   A 1 89  ? -28.951 -37.046 22.510  1.00 42.89  ? 89  VAL   A N    1 
ATOM   683  C  CA   . VAL   A 1 89  ? -27.567 -37.349 22.085  1.00 42.52  ? 89  VAL   A CA   1 
ATOM   684  C  C    . VAL   A 1 89  ? -26.621 -37.351 23.292  1.00 46.85  ? 89  VAL   A C    1 
ATOM   685  O  O    . VAL   A 1 89  ? -27.021 -36.921 24.425  1.00 44.53  ? 89  VAL   A O    1 
ATOM   686  C  CB   . VAL   A 1 89  ? -27.153 -36.254 21.095  1.00 42.70  ? 89  VAL   A CB   1 
ATOM   687  C  CG1  . VAL   A 1 89  ? -28.041 -36.253 19.875  1.00 42.50  ? 89  VAL   A CG1  1 
ATOM   688  C  CG2  . VAL   A 1 89  ? -27.135 -34.884 21.772  1.00 40.33  ? 89  VAL   A CG2  1 
ATOM   689  N  N    . ARG   A 1 90  ? -25.355 -37.672 23.018  1.00 45.39  ? 90  ARG   A N    1 
ATOM   690  C  CA   . ARG   A 1 90  ? -24.214 -37.286 23.887  1.00 40.58  ? 90  ARG   A CA   1 
ATOM   691  C  C    . ARG   A 1 90  ? -23.223 -36.434 23.114  1.00 40.46  ? 90  ARG   A C    1 
ATOM   692  O  O    . ARG   A 1 90  ? -23.114 -36.571 21.896  1.00 44.94  ? 90  ARG   A O    1 
ATOM   693  C  CB   . ARG   A 1 90  ? -23.453 -38.476 24.462  1.00 37.71  ? 90  ARG   A CB   1 
ATOM   694  C  CG   . ARG   A 1 90  ? -24.202 -39.143 25.599  1.00 44.31  ? 90  ARG   A CG   1 
ATOM   695  C  CD   . ARG   A 1 90  ? -23.309 -40.045 26.415  1.00 45.95  ? 90  ARG   A CD   1 
ATOM   696  N  NE   . ARG   A 1 90  ? -23.906 -40.352 27.704  1.00 47.32  ? 90  ARG   A NE   1 
ATOM   697  C  CZ   . ARG   A 1 90  ? -24.521 -41.491 28.014  1.00 51.02  ? 90  ARG   A CZ   1 
ATOM   698  N  NH1  . ARG   A 1 90  ? -24.663 -42.454 27.116  1.00 53.88  ? 90  ARG   A NH1  1 
ATOM   699  N  NH2  . ARG   A 1 90  ? -24.980 -41.668 29.235  1.00 43.03  ? 90  ARG   A NH2  1 
ATOM   700  N  N    . VAL   A 1 91  ? -22.492 -35.624 23.866  1.00 39.57  ? 91  VAL   A N    1 
ATOM   701  C  CA   . VAL   A 1 91  ? -21.468 -34.712 23.343  1.00 37.73  ? 91  VAL   A CA   1 
ATOM   702  C  C    . VAL   A 1 91  ? -20.145 -35.211 23.875  1.00 41.34  ? 91  VAL   A C    1 
ATOM   703  O  O    . VAL   A 1 91  ? -20.129 -35.815 24.977  1.00 37.44  ? 91  VAL   A O    1 
ATOM   704  C  CB   . VAL   A 1 91  ? -21.803 -33.255 23.682  1.00 42.42  ? 91  VAL   A CB   1 
ATOM   705  C  CG1  . VAL   A 1 91  ? -23.151 -32.924 23.065  1.00 44.08  ? 91  VAL   A CG1  1 
ATOM   706  C  CG2  . VAL   A 1 91  ? -21.765 -32.918 25.171  1.00 42.03  ? 91  VAL   A CG2  1 
ATOM   707  N  N    . GLY   A 1 92  ? -19.103 -35.017 23.070  1.00 38.58  ? 92  GLY   A N    1 
ATOM   708  C  CA   . GLY   A 1 92  ? -17.810 -35.658 23.306  1.00 38.51  ? 92  GLY   A CA   1 
ATOM   709  C  C    . GLY   A 1 92  ? -16.678 -34.994 22.557  1.00 40.82  ? 92  GLY   A C    1 
ATOM   710  O  O    . GLY   A 1 92  ? -16.929 -34.194 21.627  1.00 38.38  ? 92  GLY   A O    1 
ATOM   711  N  N    . LEU   A 1 93  ? -15.474 -35.367 22.989  1.00 43.02  ? 93  LEU   A N    1 
ATOM   712  C  CA   . LEU   A 1 93  ? -14.169 -35.088 22.372  1.00 40.10  ? 93  LEU   A CA   1 
ATOM   713  C  C    . LEU   A 1 93  ? -13.554 -36.440 21.976  1.00 42.57  ? 93  LEU   A C    1 
ATOM   714  O  O    . LEU   A 1 93  ? -13.713 -37.410 22.730  1.00 39.36  ? 93  LEU   A O    1 
ATOM   715  C  CB   . LEU   A 1 93  ? -13.339 -34.316 23.404  1.00 40.88  ? 93  LEU   A CB   1 
ATOM   716  C  CG   . LEU   A 1 93  ? -13.896 -32.945 23.803  1.00 44.16  ? 93  LEU   A CG   1 
ATOM   717  C  CD1  . LEU   A 1 93  ? -12.943 -32.193 24.730  1.00 44.49  ? 93  LEU   A CD1  1 
ATOM   718  C  CD2  . LEU   A 1 93  ? -14.207 -32.102 22.584  1.00 43.73  ? 93  LEU   A CD2  1 
ATOM   719  N  N    . SER   A 1 94  ? -12.947 -36.483 20.791  1.00 40.53  ? 94  SER   A N    1 
ATOM   720  C  CA   . SER   A 1 94  ? -12.344 -37.655 20.129  1.00 42.13  ? 94  SER   A CA   1 
ATOM   721  C  C    . SER   A 1 94  ? -10.995 -37.217 19.568  1.00 45.43  ? 94  SER   A C    1 
ATOM   722  O  O    . SER   A 1 94  ? -10.904 -36.047 19.104  1.00 44.61  ? 94  SER   A O    1 
ATOM   723  C  CB   . SER   A 1 94  ? -13.240 -38.171 19.029  1.00 46.90  ? 94  SER   A CB   1 
ATOM   724  O  OG   . SER   A 1 94  ? -12.816 -39.450 18.561  1.00 47.74  ? 94  SER   A OG   1 
ATOM   725  N  N    . ALA   A 1 95  ? -9.994  -38.103 19.590  1.00 41.17  ? 95  ALA   A N    1 
ATOM   726  C  CA   . ALA   A 1 95  ? -8.718  -37.887 18.873  1.00 40.25  ? 95  ALA   A CA   1 
ATOM   727  C  C    . ALA   A 1 95  ? -8.109  -39.228 18.455  1.00 38.04  ? 95  ALA   A C    1 
ATOM   728  O  O    . ALA   A 1 95  ? -8.592  -40.266 18.895  1.00 34.00  ? 95  ALA   A O    1 
ATOM   729  C  CB   . ALA   A 1 95  ? -7.787  -37.057 19.712  1.00 38.30  ? 95  ALA   A CB   1 
ATOM   730  N  N    . SER   A 1 96  ? -7.118  -39.184 17.571  1.00 37.11  ? 96  SER   A N    1 
ATOM   731  C  CA   . SER   A 1 96  ? -6.427  -40.377 17.037  1.00 38.84  ? 96  SER   A CA   1 
ATOM   732  C  C    . SER   A 1 96  ? -4.995  -40.032 16.637  1.00 40.70  ? 96  SER   A C    1 
ATOM   733  O  O    . SER   A 1 96  ? -4.655  -38.842 16.436  1.00 36.76  ? 96  SER   A O    1 
ATOM   734  C  CB   . SER   A 1 96  ? -7.182  -40.977 15.880  1.00 42.05  ? 96  SER   A CB   1 
ATOM   735  O  OG   . SER   A 1 96  ? -7.319  -40.049 14.810  1.00 42.69  ? 96  SER   A OG   1 
ATOM   736  N  N    . THR   A 1 97  ? -4.182  -41.078 16.571  1.00 44.97  ? 97  THR   A N    1 
ATOM   737  C  CA   . THR   A 1 97  ? -2.837  -41.098 15.953  1.00 45.60  ? 97  THR   A CA   1 
ATOM   738  C  C    . THR   A 1 97  ? -2.842  -42.320 15.051  1.00 47.05  ? 97  THR   A C    1 
ATOM   739  O  O    . THR   A 1 97  ? -3.742  -43.146 15.243  1.00 40.09  ? 97  THR   A O    1 
ATOM   740  C  CB   . THR   A 1 97  ? -1.744  -41.132 17.026  1.00 44.67  ? 97  THR   A CB   1 
ATOM   741  O  OG1  . THR   A 1 97  ? -1.832  -42.359 17.753  1.00 43.81  ? 97  THR   A OG1  1 
ATOM   742  C  CG2  . THR   A 1 97  ? -1.891  -39.973 17.980  1.00 44.96  ? 97  THR   A CG2  1 
ATOM   743  N  N    . GLY   A 1 98  ? -1.912  -42.391 14.098  1.00 50.96  ? 98  GLY   A N    1 
ATOM   744  C  CA   . GLY   A 1 98  ? -1.758  -43.549 13.201  1.00 49.94  ? 98  GLY   A CA   1 
ATOM   745  C  C    . GLY   A 1 98  ? -0.299  -43.906 13.064  1.00 48.76  ? 98  GLY   A C    1 
ATOM   746  O  O    . GLY   A 1 98  ? 0.334   -44.163 14.111  1.00 45.05  ? 98  GLY   A O    1 
ATOM   747  N  N    . LEU   A 1 99  ? 0.219   -43.886 11.832  1.00 40.51  ? 99  LEU   A N    1 
ATOM   748  C  CA   . LEU   A 1 99  ? 1.667   -44.005 11.604  1.00 40.38  ? 99  LEU   A CA   1 
ATOM   749  C  C    . LEU   A 1 99  ? 2.350   -42.800 12.286  1.00 40.46  ? 99  LEU   A C    1 
ATOM   750  O  O    . LEU   A 1 99  ? 3.406   -42.999 12.933  1.00 41.30  ? 99  LEU   A O    1 
ATOM   751  C  CB   . LEU   A 1 99  ? 1.964   -44.107 10.102  1.00 39.66  ? 99  LEU   A CB   1 
ATOM   752  C  CG   . LEU   A 1 99  ? 3.448   -44.092 9.709   1.00 43.72  ? 99  LEU   A CG   1 
ATOM   753  C  CD1  . LEU   A 1 99  ? 4.182   -45.335 10.179  1.00 41.56  ? 99  LEU   A CD1  1 
ATOM   754  C  CD2  . LEU   A 1 99  ? 3.610   -43.936 8.210   1.00 42.25  ? 99  LEU   A CD2  1 
ATOM   755  N  N    . TYR   A 1 100 ? 1.811   -41.590 12.125  1.00 44.24  ? 100 TYR   A N    1 
ATOM   756  C  CA   . TYR   A 1 100 ? 2.322   -40.353 12.790  1.00 44.38  ? 100 TYR   A CA   1 
ATOM   757  C  C    . TYR   A 1 100 ? 1.425   -39.963 13.993  1.00 37.66  ? 100 TYR   A C    1 
ATOM   758  O  O    . TYR   A 1 100 ? 0.321   -40.484 14.154  1.00 37.31  ? 100 TYR   A O    1 
ATOM   759  C  CB   . TYR   A 1 100 ? 2.476   -39.242 11.758  1.00 43.80  ? 100 TYR   A CB   1 
ATOM   760  C  CG   . TYR   A 1 100 ? 3.346   -39.592 10.583  1.00 47.05  ? 100 TYR   A CG   1 
ATOM   761  C  CD1  . TYR   A 1 100 ? 4.676   -39.954 10.773  1.00 48.52  ? 100 TYR   A CD1  1 
ATOM   762  C  CD2  . TYR   A 1 100 ? 2.875   -39.467 9.282   1.00 44.77  ? 100 TYR   A CD2  1 
ATOM   763  C  CE1  . TYR   A 1 100 ? 5.501   -40.265 9.703   1.00 43.25  ? 100 TYR   A CE1  1 
ATOM   764  C  CE2  . TYR   A 1 100 ? 3.690   -39.765 8.201   1.00 47.51  ? 100 TYR   A CE2  1 
ATOM   765  C  CZ   . TYR   A 1 100 ? 5.002   -40.175 8.411   1.00 49.35  ? 100 TYR   A CZ   1 
ATOM   766  O  OH   . TYR   A 1 100 ? 5.815   -40.480 7.349   1.00 52.65  ? 100 TYR   A OH   1 
ATOM   767  N  N    . LYS   A 1 101 ? 1.910   -39.078 14.854  1.00 40.29  ? 101 LYS   A N    1 
ATOM   768  C  CA   . LYS   A 1 101 ? 1.433   -38.972 16.257  1.00 43.59  ? 101 LYS   A CA   1 
ATOM   769  C  C    . LYS   A 1 101 ? 1.515   -37.522 16.738  1.00 41.19  ? 101 LYS   A C    1 
ATOM   770  O  O    . LYS   A 1 101 ? 2.160   -36.706 16.078  1.00 39.75  ? 101 LYS   A O    1 
ATOM   771  C  CB   . LYS   A 1 101 ? 2.273   -39.891 17.157  1.00 49.57  ? 101 LYS   A CB   1 
ATOM   772  C  CG   . LYS   A 1 101 ? 3.776   -39.764 16.971  1.00 56.35  ? 101 LYS   A CG   1 
ATOM   773  C  CD   . LYS   A 1 101 ? 4.553   -41.003 17.334  1.00 66.93  ? 101 LYS   A CD   1 
ATOM   774  C  CE   . LYS   A 1 101 ? 4.318   -42.163 16.385  1.00 68.71  ? 101 LYS   A CE   1 
ATOM   775  N  NZ   . LYS   A 1 101 ? 5.585   -42.885 16.088  1.00 64.85  ? 101 LYS   A NZ   1 
ATOM   776  N  N    . GLU   A 1 102 ? 0.840   -37.234 17.848  1.00 37.67  ? 102 GLU   A N    1 
ATOM   777  C  CA   . GLU   A 1 102 ? 0.779   -35.904 18.491  1.00 41.60  ? 102 GLU   A CA   1 
ATOM   778  C  C    . GLU   A 1 102 ? 0.140   -36.126 19.860  1.00 42.40  ? 102 GLU   A C    1 
ATOM   779  O  O    . GLU   A 1 102 ? -0.606  -37.118 20.010  1.00 42.28  ? 102 GLU   A O    1 
ATOM   780  C  CB   . GLU   A 1 102 ? 0.006   -34.898 17.617  1.00 43.16  ? 102 GLU   A CB   1 
ATOM   781  C  CG   . GLU   A 1 102 ? -1.487  -35.174 17.551  1.00 43.34  ? 102 GLU   A CG   1 
ATOM   782  C  CD   . GLU   A 1 102 ? -2.300  -34.478 16.466  1.00 45.47  ? 102 GLU   A CD   1 
ATOM   783  O  OE1  . GLU   A 1 102 ? -1.733  -34.056 15.433  1.00 43.87  ? 102 GLU   A OE1  1 
ATOM   784  O  OE2  . GLU   A 1 102 ? -3.527  -34.418 16.634  1.00 42.47  ? 102 GLU   A OE2  1 
ATOM   785  N  N    . THR   A 1 103 ? 0.476   -35.298 20.848  1.00 43.79  ? 103 THR   A N    1 
ATOM   786  C  CA   . THR   A 1 103 ? -0.348  -35.160 22.074  1.00 43.44  ? 103 THR   A CA   1 
ATOM   787  C  C    . THR   A 1 103 ? -1.700  -34.625 21.588  1.00 48.32  ? 103 THR   A C    1 
ATOM   788  O  O    . THR   A 1 103 ? -1.722  -33.835 20.598  1.00 43.03  ? 103 THR   A O    1 
ATOM   789  C  CB   . THR   A 1 103 ? 0.371   -34.328 23.146  1.00 46.46  ? 103 THR   A CB   1 
ATOM   790  O  OG1  . THR   A 1 103 ? 0.862   -33.112 22.596  1.00 52.47  ? 103 THR   A OG1  1 
ATOM   791  C  CG2  . THR   A 1 103 ? 1.591   -35.010 23.714  1.00 45.36  ? 103 THR   A CG2  1 
ATOM   792  N  N    . ASN   A 1 104 ? -2.786  -35.151 22.157  1.00 44.78  ? 104 ASN   A N    1 
ATOM   793  C  CA   . ASN   A 1 104 ? -4.160  -34.633 21.969  1.00 42.97  ? 104 ASN   A CA   1 
ATOM   794  C  C    . ASN   A 1 104 ? -4.668  -34.220 23.350  1.00 39.95  ? 104 ASN   A C    1 
ATOM   795  O  O    . ASN   A 1 104 ? -5.546  -34.883 23.912  1.00 40.28  ? 104 ASN   A O    1 
ATOM   796  C  CB   . ASN   A 1 104 ? -5.029  -35.633 21.206  1.00 42.60  ? 104 ASN   A CB   1 
ATOM   797  C  CG   . ASN   A 1 104 ? -4.516  -35.839 19.799  1.00 44.51  ? 104 ASN   A CG   1 
ATOM   798  O  OD1  . ASN   A 1 104 ? -4.065  -36.932 19.467  1.00 51.76  ? 104 ASN   A OD1  1 
ATOM   799  N  ND2  . ASN   A 1 104 ? -4.599  -34.816 18.966  1.00 35.68  ? 104 ASN   A ND2  1 
ATOM   800  N  N    . THR   A 1 105 ? -4.081  -33.153 23.867  1.00 44.51  ? 105 THR   A N    1 
ATOM   801  C  CA   . THR   A 1 105 ? -4.295  -32.659 25.243  1.00 44.45  ? 105 THR   A CA   1 
ATOM   802  C  C    . THR   A 1 105 ? -5.450  -31.653 25.252  1.00 45.35  ? 105 THR   A C    1 
ATOM   803  O  O    . THR   A 1 105 ? -5.385  -30.653 24.504  1.00 45.55  ? 105 THR   A O    1 
ATOM   804  C  CB   . THR   A 1 105 ? -2.984  -32.099 25.811  1.00 43.30  ? 105 THR   A CB   1 
ATOM   805  O  OG1  . THR   A 1 105 ? -2.025  -33.147 25.729  1.00 42.03  ? 105 THR   A OG1  1 
ATOM   806  C  CG2  . THR   A 1 105 ? -3.117  -31.649 27.247  1.00 44.68  ? 105 THR   A CG2  1 
ATOM   807  N  N    . ILE   A 1 106 ? -6.440  -31.907 26.113  1.00 47.75  ? 106 ILE   A N    1 
ATOM   808  C  CA   . ILE   A 1 106 ? -7.552  -30.972 26.446  1.00 49.35  ? 106 ILE   A CA   1 
ATOM   809  C  C    . ILE   A 1 106 ? -7.341  -30.353 27.847  1.00 50.13  ? 106 ILE   A C    1 
ATOM   810  O  O    . ILE   A 1 106 ? -7.265  -31.096 28.853  1.00 46.94  ? 106 ILE   A O    1 
ATOM   811  C  CB   . ILE   A 1 106 ? -8.872  -31.739 26.313  1.00 44.57  ? 106 ILE   A CB   1 
ATOM   812  C  CG1  . ILE   A 1 106 ? -8.969  -32.419 24.950  1.00 40.31  ? 106 ILE   A CG1  1 
ATOM   813  C  CG2  . ILE   A 1 106 ? -10.070 -30.828 26.569  1.00 45.54  ? 106 ILE   A CG2  1 
ATOM   814  C  CD1  . ILE   A 1 106 ? -9.235  -31.474 23.832  1.00 38.15  ? 106 ILE   A CD1  1 
ATOM   815  N  N    . LEU   A 1 107 ? -7.285  -29.022 27.914  1.00 49.59  ? 107 LEU   A N    1 
ATOM   816  C  CA   . LEU   A 1 107 ? -6.988  -28.241 29.153  1.00 47.88  ? 107 LEU   A CA   1 
ATOM   817  C  C    . LEU   A 1 107 ? -8.296  -27.745 29.785  1.00 46.36  ? 107 LEU   A C    1 
ATOM   818  O  O    . LEU   A 1 107 ? -8.300  -27.471 30.990  1.00 46.67  ? 107 LEU   A O    1 
ATOM   819  C  CB   . LEU   A 1 107 ? -6.082  -27.054 28.817  1.00 45.94  ? 107 LEU   A CB   1 
ATOM   820  C  CG   . LEU   A 1 107 ? -4.593  -27.357 28.635  1.00 56.54  ? 107 LEU   A CG   1 
ATOM   821  C  CD1  . LEU   A 1 107 ? -4.347  -28.192 27.395  1.00 64.73  ? 107 LEU   A CD1  1 
ATOM   822  C  CD2  . LEU   A 1 107 ? -3.787  -26.071 28.519  1.00 62.49  ? 107 LEU   A CD2  1 
ATOM   823  N  N    . SER   A 1 108 ? -9.348  -27.592 28.989  1.00 44.34  ? 108 SER   A N    1 
ATOM   824  C  CA   . SER   A 1 108 ? -10.695 -27.167 29.438  1.00 42.86  ? 108 SER   A CA   1 
ATOM   825  C  C    . SER   A 1 108 ? -11.729 -27.503 28.365  1.00 44.24  ? 108 SER   A C    1 
ATOM   826  O  O    . SER   A 1 108 ? -11.396 -27.445 27.145  1.00 40.70  ? 108 SER   A O    1 
ATOM   827  C  CB   . SER   A 1 108 ? -10.728 -25.679 29.758  1.00 41.99  ? 108 SER   A CB   1 
ATOM   828  O  OG   . SER   A 1 108 ? -10.516 -24.875 28.595  1.00 34.91  ? 108 SER   A OG   1 
ATOM   829  N  N    . TRP   A 1 109 ? -12.967 -27.722 28.799  1.00 45.31  ? 109 TRP   A N    1 
ATOM   830  C  CA   . TRP   A 1 109 ? -14.111 -27.977 27.896  1.00 40.49  ? 109 TRP   A CA   1 
ATOM   831  C  C    . TRP   A 1 109 ? -15.347 -27.406 28.570  1.00 42.39  ? 109 TRP   A C    1 
ATOM   832  O  O    . TRP   A 1 109 ? -15.560 -27.716 29.744  1.00 42.11  ? 109 TRP   A O    1 
ATOM   833  C  CB   . TRP   A 1 109 ? -14.215 -29.486 27.641  1.00 41.17  ? 109 TRP   A CB   1 
ATOM   834  C  CG   . TRP   A 1 109 ? -15.343 -29.969 26.777  1.00 40.85  ? 109 TRP   A CG   1 
ATOM   835  C  CD1  . TRP   A 1 109 ? -15.972 -29.286 25.776  1.00 38.33  ? 109 TRP   A CD1  1 
ATOM   836  C  CD2  . TRP   A 1 109 ? -15.914 -31.296 26.777  1.00 38.33  ? 109 TRP   A CD2  1 
ATOM   837  N  NE1  . TRP   A 1 109 ? -16.892 -30.096 25.156  1.00 41.72  ? 109 TRP   A NE1  1 
ATOM   838  C  CE2  . TRP   A 1 109 ? -16.909 -31.322 25.777  1.00 38.20  ? 109 TRP   A CE2  1 
ATOM   839  C  CE3  . TRP   A 1 109 ? -15.714 -32.451 27.540  1.00 41.91  ? 109 TRP   A CE3  1 
ATOM   840  C  CZ2  . TRP   A 1 109 ? -17.705 -32.448 25.536  1.00 42.48  ? 109 TRP   A CZ2  1 
ATOM   841  C  CZ3  . TRP   A 1 109 ? -16.485 -33.578 27.291  1.00 45.50  ? 109 TRP   A CZ3  1 
ATOM   842  C  CH2  . TRP   A 1 109 ? -17.465 -33.578 26.290  1.00 46.17  ? 109 TRP   A CH2  1 
ATOM   843  N  N    . SER   A 1 110 ? -16.115 -26.592 27.859  1.00 40.47  ? 110 SER   A N    1 
ATOM   844  C  CA   . SER   A 1 110 ? -17.456 -26.162 28.301  1.00 44.58  ? 110 SER   A CA   1 
ATOM   845  C  C    . SER   A 1 110 ? -18.483 -26.437 27.198  1.00 47.35  ? 110 SER   A C    1 
ATOM   846  O  O    . SER   A 1 110 ? -18.083 -26.587 26.027  1.00 46.96  ? 110 SER   A O    1 
ATOM   847  C  CB   . SER   A 1 110 ? -17.448 -24.731 28.634  1.00 43.89  ? 110 SER   A CB   1 
ATOM   848  O  OG   . SER   A 1 110 ? -17.655 -24.015 27.444  1.00 49.42  ? 110 SER   A OG   1 
ATOM   849  N  N    . PHE   A 1 111 ? -19.764 -26.422 27.560  1.00 41.66  ? 111 PHE   A N    1 
ATOM   850  C  CA   . PHE   A 1 111 ? -20.885 -26.794 26.671  1.00 35.61  ? 111 PHE   A CA   1 
ATOM   851  C  C    . PHE   A 1 111 ? -22.160 -26.240 27.273  1.00 38.42  ? 111 PHE   A C    1 
ATOM   852  O  O    . PHE   A 1 111 ? -22.323 -26.371 28.497  1.00 40.66  ? 111 PHE   A O    1 
ATOM   853  C  CB   . PHE   A 1 111 ? -21.047 -28.306 26.538  1.00 35.54  ? 111 PHE   A CB   1 
ATOM   854  C  CG   . PHE   A 1 111 ? -22.202 -28.720 25.658  1.00 38.09  ? 111 PHE   A CG   1 
ATOM   855  C  CD1  . PHE   A 1 111 ? -22.060 -28.799 24.277  1.00 39.83  ? 111 PHE   A CD1  1 
ATOM   856  C  CD2  . PHE   A 1 111 ? -23.444 -29.021 26.206  1.00 41.25  ? 111 PHE   A CD2  1 
ATOM   857  C  CE1  . PHE   A 1 111 ? -23.113 -29.188 23.462  1.00 37.53  ? 111 PHE   A CE1  1 
ATOM   858  C  CE2  . PHE   A 1 111 ? -24.504 -29.382 25.386  1.00 42.66  ? 111 PHE   A CE2  1 
ATOM   859  C  CZ   . PHE   A 1 111 ? -24.340 -29.466 24.016  1.00 40.94  ? 111 PHE   A CZ   1 
ATOM   860  N  N    . THR   A 1 112 ? -22.997 -25.642 26.425  1.00 38.82  ? 112 THR   A N    1 
ATOM   861  C  CA   . THR   A 1 112 ? -24.356 -25.172 26.751  1.00 42.68  ? 112 THR   A CA   1 
ATOM   862  C  C    . THR   A 1 112 ? -25.334 -25.593 25.647  1.00 47.18  ? 112 THR   A C    1 
ATOM   863  O  O    . THR   A 1 112 ? -24.998 -25.461 24.472  1.00 52.65  ? 112 THR   A O    1 
ATOM   864  C  CB   . THR   A 1 112 ? -24.364 -23.655 26.947  1.00 45.96  ? 112 THR   A CB   1 
ATOM   865  O  OG1  . THR   A 1 112 ? -23.451 -23.335 28.000  1.00 52.44  ? 112 THR   A OG1  1 
ATOM   866  C  CG2  . THR   A 1 112 ? -25.741 -23.139 27.294  1.00 51.41  ? 112 THR   A CG2  1 
ATOM   867  N  N    . SER   A 1 113 ? -26.534 -26.009 26.045  1.00 48.64  ? 113 SER   A N    1 
ATOM   868  C  CA   . SER   A 1 113 ? -27.666 -26.399 25.183  1.00 44.62  ? 113 SER   A CA   1 
ATOM   869  C  C    . SER   A 1 113 ? -28.931 -25.798 25.779  1.00 50.37  ? 113 SER   A C    1 
ATOM   870  O  O    . SER   A 1 113 ? -29.049 -25.929 27.006  1.00 46.26  ? 113 SER   A O    1 
ATOM   871  C  CB   . SER   A 1 113 ? -27.766 -27.871 25.207  1.00 48.69  ? 113 SER   A CB   1 
ATOM   872  O  OG   . SER   A 1 113 ? -28.965 -28.304 24.607  1.00 55.37  ? 113 SER   A OG   1 
ATOM   873  N  N    . LYS   A 1 114 ? -29.842 -25.250 24.964  1.00 43.00  ? 114 LYS   A N    1 
ATOM   874  C  CA   . LYS   A 1 114 ? -31.126 -24.671 25.421  1.00 45.47  ? 114 LYS   A CA   1 
ATOM   875  C  C    . LYS   A 1 114 ? -32.230 -25.041 24.445  1.00 46.52  ? 114 LYS   A C    1 
ATOM   876  O  O    . LYS   A 1 114 ? -31.963 -24.991 23.273  1.00 49.07  ? 114 LYS   A O    1 
ATOM   877  C  CB   . LYS   A 1 114 ? -31.117 -23.143 25.481  1.00 50.08  ? 114 LYS   A CB   1 
ATOM   878  C  CG   . LYS   A 1 114 ? -29.965 -22.545 26.261  1.00 60.70  ? 114 LYS   A CG   1 
ATOM   879  C  CD   . LYS   A 1 114 ? -30.100 -21.073 26.567  1.00 63.38  ? 114 LYS   A CD   1 
ATOM   880  C  CE   . LYS   A 1 114 ? -28.845 -20.524 27.223  1.00 70.36  ? 114 LYS   A CE   1 
ATOM   881  N  NZ   . LYS   A 1 114 ? -29.142 -19.842 28.503  1.00 74.17  ? 114 LYS   A NZ   1 
ATOM   882  N  N    . LEU   A 1 115 ? -33.416 -25.386 24.954  1.00 53.30  ? 115 LEU   A N    1 
ATOM   883  C  CA   . LEU   A 1 115 ? -34.694 -25.445 24.197  1.00 57.57  ? 115 LEU   A CA   1 
ATOM   884  C  C    . LEU   A 1 115 ? -35.628 -24.368 24.734  1.00 62.40  ? 115 LEU   A C    1 
ATOM   885  O  O    . LEU   A 1 115 ? -35.779 -24.318 25.938  1.00 64.09  ? 115 LEU   A O    1 
ATOM   886  C  CB   . LEU   A 1 115 ? -35.311 -26.822 24.395  1.00 52.16  ? 115 LEU   A CB   1 
ATOM   887  C  CG   . LEU   A 1 115 ? -34.403 -27.970 23.977  1.00 48.79  ? 115 LEU   A CG   1 
ATOM   888  C  CD1  . LEU   A 1 115 ? -35.091 -29.287 24.200  1.00 50.43  ? 115 LEU   A CD1  1 
ATOM   889  C  CD2  . LEU   A 1 115 ? -33.997 -27.857 22.522  1.00 50.44  ? 115 LEU   A CD2  1 
ATOM   890  N  N    . LYS   A 1 116 ? -36.173 -23.513 23.868  1.00 73.46  ? 116 LYS   A N    1 
ATOM   891  C  CA   . LYS   A 1 116 ? -37.204 -22.505 24.228  1.00 71.34  ? 116 LYS   A CA   1 
ATOM   892  C  C    . LYS   A 1 116 ? -38.471 -22.872 23.459  1.00 74.33  ? 116 LYS   A C    1 
ATOM   893  O  O    . LYS   A 1 116 ? -38.403 -22.891 22.232  1.00 72.88  ? 116 LYS   A O    1 
ATOM   894  C  CB   . LYS   A 1 116 ? -36.677 -21.099 23.941  1.00 74.37  ? 116 LYS   A CB   1 
ATOM   895  C  CG   . LYS   A 1 116 ? -35.304 -20.781 24.545  1.00 80.73  ? 116 LYS   A CG   1 
ATOM   896  C  CD   . LYS   A 1 116 ? -34.983 -19.283 24.575  1.00 86.11  ? 116 LYS   A CD   1 
ATOM   897  C  CE   . LYS   A 1 116 ? -33.933 -18.856 25.581  1.00 85.33  ? 116 LYS   A CE   1 
ATOM   898  N  NZ   . LYS   A 1 116 ? -32.654 -18.509 24.914  1.00 73.77  ? 116 LYS   A NZ   1 
ATOM   899  N  N    . SER   A 1 117 ? -39.443 -23.386 24.215  1.00 98.27  ? 117 SER   A N    1 
ATOM   900  C  CA   . SER   A 1 117 ? -40.700 -24.037 23.761  1.00 109.22 ? 117 SER   A CA   1 
ATOM   901  C  C    . SER   A 1 117 ? -41.726 -23.107 23.122  1.00 117.47 ? 117 SER   A C    1 
ATOM   902  O  O    . SER   A 1 117 ? -41.692 -21.898 23.354  1.00 80.22  ? 117 SER   A O    1 
ATOM   903  C  CB   . SER   A 1 117 ? -41.332 -24.813 24.885  1.00 109.28 ? 117 SER   A CB   1 
ATOM   904  O  OG   . SER   A 1 117 ? -42.005 -25.966 24.409  1.00 107.02 ? 117 SER   A OG   1 
ATOM   905  N  N    . ASN   A 1 118 ? -42.571 -23.729 22.297  1.00 146.93 ? 118 ASN   A N    1 
ATOM   906  C  CA   . ASN   A 1 118 ? -43.716 -23.094 21.605  1.00 154.17 ? 118 ASN   A CA   1 
ATOM   907  C  C    . ASN   A 1 118 ? -45.010 -23.603 22.246  1.00 161.35 ? 118 ASN   A C    1 
ATOM   908  O  O    . ASN   A 1 118 ? -45.996 -22.862 22.255  1.00 157.87 ? 118 ASN   A O    1 
ATOM   909  C  CB   . ASN   A 1 118 ? -43.773 -23.498 20.136  1.00 152.38 ? 118 ASN   A CB   1 
ATOM   910  C  CG   . ASN   A 1 118 ? -45.192 -23.467 19.619  1.00 151.51 ? 118 ASN   A CG   1 
ATOM   911  O  OD1  . ASN   A 1 118 ? -45.632 -24.385 18.933  1.00 137.64 ? 118 ASN   A OD1  1 
ATOM   912  N  ND2  . ASN   A 1 118 ? -45.919 -22.419 19.965  1.00 149.45 ? 118 ASN   A ND2  1 
ATOM   913  N  N    . SER   A 1 119 ? -45.016 -24.867 22.670  1.00 168.04 ? 119 SER   A N    1 
ATOM   914  C  CA   . SER   A 1 119 ? -46.199 -25.488 23.317  1.00 160.34 ? 119 SER   A CA   1 
ATOM   915  C  C    . SER   A 1 119 ? -46.479 -24.825 24.661  1.00 157.19 ? 119 SER   A C    1 
ATOM   916  O  O    . SER   A 1 119 ? -47.645 -24.490 24.936  1.00 132.22 ? 119 SER   A O    1 
ATOM   917  C  CB   . SER   A 1 119 ? -45.911 -26.936 23.561  1.00 149.45 ? 119 SER   A CB   1 
ATOM   918  O  OG   . SER   A 1 119 ? -44.876 -27.061 24.531  1.00 148.61 ? 119 SER   A OG   1 
ATOM   919  N  N    . THR   A 1 120 ? -45.418 -24.644 25.447  1.00 169.27 ? 120 THR   A N    1 
ATOM   920  C  CA   . THR   A 1 120 ? -45.526 -24.099 26.825  1.00 175.94 ? 120 THR   A CA   1 
ATOM   921  C  C    . THR   A 1 120 ? -44.769 -22.778 26.961  1.00 169.91 ? 120 THR   A C    1 
ATOM   922  O  O    . THR   A 1 120 ? -44.880 -22.148 28.022  1.00 164.16 ? 120 THR   A O    1 
ATOM   923  C  CB   . THR   A 1 120 ? -45.004 -25.117 27.846  1.00 172.76 ? 120 THR   A CB   1 
ATOM   924  O  OG1  . THR   A 1 120 ? -43.918 -25.832 27.254  1.00 169.14 ? 120 THR   A OG1  1 
ATOM   925  C  CG2  . THR   A 1 120 ? -46.071 -26.083 28.315  1.00 161.26 ? 120 THR   A CG2  1 
ATOM   926  N  N    . HIS   A 1 121 ? -44.018 -22.383 25.938  1.00 169.65 ? 121 HIS   A N    1 
ATOM   927  C  CA   . HIS   A 1 121 ? -43.274 -21.100 26.028  1.00 175.02 ? 121 HIS   A CA   1 
ATOM   928  C  C    . HIS   A 1 121 ? -42.375 -21.048 27.278  1.00 177.03 ? 121 HIS   A C    1 
ATOM   929  O  O    . HIS   A 1 121 ? -42.399 -20.014 27.972  1.00 165.93 ? 121 HIS   A O    1 
ATOM   930  C  CB   . HIS   A 1 121 ? -44.222 -19.913 25.804  1.00 159.88 ? 121 HIS   A CB   1 
ATOM   931  C  CG   . HIS   A 1 121 ? -44.322 -19.527 24.363  1.00 148.37 ? 121 HIS   A CG   1 
ATOM   932  N  ND1  . HIS   A 1 121 ? -44.445 -20.461 23.360  1.00 126.77 ? 121 HIS   A ND1  1 
ATOM   933  C  CD2  . HIS   A 1 121 ? -44.299 -18.321 23.752  1.00 133.98 ? 121 HIS   A CD2  1 
ATOM   934  C  CE1  . HIS   A 1 121 ? -44.501 -19.846 22.198  1.00 125.60 ? 121 HIS   A CE1  1 
ATOM   935  N  NE2  . HIS   A 1 121 ? -44.412 -18.537 22.409  1.00 121.59 ? 121 HIS   A NE2  1 
ATOM   936  N  N    . GLU   A 1 122 ? -41.640 -22.139 27.554  1.00 174.44 ? 122 GLU   A N    1 
ATOM   937  C  CA   . GLU   A 1 122 ? -40.679 -22.247 28.695  1.00 142.13 ? 122 GLU   A CA   1 
ATOM   938  C  C    . GLU   A 1 122 ? -39.411 -22.996 28.245  1.00 120.75 ? 122 GLU   A C    1 
ATOM   939  O  O    . GLU   A 1 122 ? -39.512 -23.836 27.347  1.00 108.53 ? 122 GLU   A O    1 
ATOM   940  C  CB   . GLU   A 1 122 ? -41.376 -22.808 29.926  1.00 145.24 ? 122 GLU   A CB   1 
ATOM   941  C  CG   . GLU   A 1 122 ? -42.153 -21.746 30.674  1.00 139.99 ? 122 GLU   A CG   1 
ATOM   942  C  CD   . GLU   A 1 122 ? -41.288 -20.658 31.285  1.00 134.95 ? 122 GLU   A CD   1 
ATOM   943  O  OE1  . GLU   A 1 122 ? -41.508 -20.337 32.464  1.00 115.17 ? 122 GLU   A OE1  1 
ATOM   944  O  OE2  . GLU   A 1 122 ? -40.403 -20.137 30.580  1.00 115.92 ? 122 GLU   A OE2  1 
ATOM   945  N  N    . THR   A 1 123 ? -38.281 -22.766 28.915  1.00 96.92  ? 123 THR   A N    1 
ATOM   946  C  CA   . THR   A 1 123 ? -36.971 -23.274 28.431  1.00 84.50  ? 123 THR   A CA   1 
ATOM   947  C  C    . THR   A 1 123 ? -36.368 -24.411 29.262  1.00 78.48  ? 123 THR   A C    1 
ATOM   948  O  O    . THR   A 1 123 ? -36.570 -24.400 30.462  1.00 75.45  ? 123 THR   A O    1 
ATOM   949  C  CB   . THR   A 1 123 ? -35.986 -22.095 28.400  1.00 91.99  ? 123 THR   A CB   1 
ATOM   950  O  OG1  . THR   A 1 123 ? -35.067 -22.139 29.487  1.00 97.02  ? 123 THR   A OG1  1 
ATOM   951  C  CG2  . THR   A 1 123 ? -36.658 -20.742 28.469  1.00 87.82  ? 123 THR   A CG2  1 
ATOM   952  N  N    . ASN   A 1 124 ? -35.713 -25.384 28.603  1.00 66.21  ? 124 ASN   A N    1 
ATOM   953  C  CA   . ASN   A 1 124 ? -34.868 -26.451 29.220  1.00 58.53  ? 124 ASN   A CA   1 
ATOM   954  C  C    . ASN   A 1 124 ? -33.395 -26.203 28.878  1.00 59.11  ? 124 ASN   A C    1 
ATOM   955  O  O    . ASN   A 1 124 ? -33.149 -25.688 27.800  1.00 57.23  ? 124 ASN   A O    1 
ATOM   956  C  CB   . ASN   A 1 124 ? -35.264 -27.856 28.769  1.00 63.27  ? 124 ASN   A CB   1 
ATOM   957  C  CG   . ASN   A 1 124 ? -36.692 -28.154 29.155  1.00 68.06  ? 124 ASN   A CG   1 
ATOM   958  O  OD1  . ASN   A 1 124 ? -37.287 -27.393 29.915  1.00 60.81  ? 124 ASN   A OD1  1 
ATOM   959  N  ND2  . ASN   A 1 124 ? -37.255 -29.220 28.608  1.00 75.58  ? 124 ASN   A ND2  1 
ATOM   960  N  N    . ALA   A 1 125 ? -32.451 -26.556 29.757  1.00 53.47  ? 125 ALA   A N    1 
ATOM   961  C  CA   . ALA   A 1 125 ? -31.052 -26.082 29.659  1.00 51.91  ? 125 ALA   A CA   1 
ATOM   962  C  C    . ALA   A 1 125 ? -30.071 -26.994 30.404  1.00 49.44  ? 125 ALA   A C    1 
ATOM   963  O  O    . ALA   A 1 125 ? -30.383 -27.431 31.537  1.00 47.63  ? 125 ALA   A O    1 
ATOM   964  C  CB   . ALA   A 1 125 ? -30.941 -24.660 30.167  1.00 47.01  ? 125 ALA   A CB   1 
ATOM   965  N  N    . LEU   A 1 126 ? -28.903 -27.196 29.788  1.00 42.03  ? 126 LEU   A N    1 
ATOM   966  C  CA   . LEU   A 1 126 ? -27.747 -27.915 30.365  1.00 42.56  ? 126 LEU   A CA   1 
ATOM   967  C  C    . LEU   A 1 126 ? -26.482 -27.123 30.048  1.00 40.72  ? 126 LEU   A C    1 
ATOM   968  O  O    . LEU   A 1 126 ? -26.347 -26.658 28.942  1.00 42.92  ? 126 LEU   A O    1 
ATOM   969  C  CB   . LEU   A 1 126 ? -27.673 -29.330 29.793  1.00 38.07  ? 126 LEU   A CB   1 
ATOM   970  C  CG   . LEU   A 1 126 ? -26.430 -30.110 30.201  1.00 41.96  ? 126 LEU   A CG   1 
ATOM   971  C  CD1  . LEU   A 1 126 ? -26.557 -30.684 31.603  1.00 44.57  ? 126 LEU   A CD1  1 
ATOM   972  C  CD2  . LEU   A 1 126 ? -26.170 -31.210 29.199  1.00 44.82  ? 126 LEU   A CD2  1 
ATOM   973  N  N    . HIS   A 1 127 ? -25.636 -26.945 31.045  1.00 39.87  ? 127 HIS   A N    1 
ATOM   974  C  CA   . HIS   A 1 127 ? -24.338 -26.247 30.953  1.00 43.46  ? 127 HIS   A CA   1 
ATOM   975  C  C    . HIS   A 1 127 ? -23.389 -27.043 31.822  1.00 40.95  ? 127 HIS   A C    1 
ATOM   976  O  O    . HIS   A 1 127 ? -23.753 -27.273 32.982  1.00 46.31  ? 127 HIS   A O    1 
ATOM   977  C  CB   . HIS   A 1 127 ? -24.434 -24.773 31.420  1.00 45.02  ? 127 HIS   A CB   1 
ATOM   978  C  CG   . HIS   A 1 127 ? -23.114 -24.072 31.514  1.00 48.10  ? 127 HIS   A CG   1 
ATOM   979  N  ND1  . HIS   A 1 127 ? -22.310 -23.825 30.392  1.00 45.95  ? 127 HIS   A ND1  1 
ATOM   980  C  CD2  . HIS   A 1 127 ? -22.413 -23.626 32.593  1.00 54.32  ? 127 HIS   A CD2  1 
ATOM   981  C  CE1  . HIS   A 1 127 ? -21.195 -23.214 30.785  1.00 54.03  ? 127 HIS   A CE1  1 
ATOM   982  N  NE2  . HIS   A 1 127 ? -21.225 -23.083 32.140  1.00 51.96  ? 127 HIS   A NE2  1 
ATOM   983  N  N    . PHE   A 1 128 ? -22.270 -27.494 31.273  1.00 43.20  ? 128 PHE   A N    1 
ATOM   984  C  CA   . PHE   A 1 128 ? -21.106 -27.929 32.085  1.00 43.72  ? 128 PHE   A CA   1 
ATOM   985  C  C    . PHE   A 1 128 ? -19.873 -27.111 31.671  1.00 44.83  ? 128 PHE   A C    1 
ATOM   986  O  O    . PHE   A 1 128 ? -19.827 -26.547 30.546  1.00 40.82  ? 128 PHE   A O    1 
ATOM   987  C  CB   . PHE   A 1 128 ? -20.940 -29.448 32.031  1.00 43.61  ? 128 PHE   A CB   1 
ATOM   988  C  CG   . PHE   A 1 128 ? -20.682 -30.016 30.667  1.00 48.29  ? 128 PHE   A CG   1 
ATOM   989  C  CD1  . PHE   A 1 128 ? -19.404 -30.009 30.132  1.00 46.88  ? 128 PHE   A CD1  1 
ATOM   990  C  CD2  . PHE   A 1 128 ? -21.711 -30.574 29.919  1.00 47.87  ? 128 PHE   A CD2  1 
ATOM   991  C  CE1  . PHE   A 1 128 ? -19.163 -30.540 28.871  1.00 47.39  ? 128 PHE   A CE1  1 
ATOM   992  C  CE2  . PHE   A 1 128 ? -21.462 -31.121 28.668  1.00 43.93  ? 128 PHE   A CE2  1 
ATOM   993  C  CZ   . PHE   A 1 128 ? -20.190 -31.082 28.140  1.00 43.60  ? 128 PHE   A CZ   1 
ATOM   994  N  N    . MET   A 1 129 ? -18.940 -26.988 32.612  1.00 42.74  ? 129 MET   A N    1 
ATOM   995  C  CA   . MET   A 1 129 ? -17.605 -26.393 32.416  1.00 43.43  ? 129 MET   A CA   1 
ATOM   996  C  C    . MET   A 1 129 ? -16.583 -27.187 33.232  1.00 40.58  ? 129 MET   A C    1 
ATOM   997  O  O    . MET   A 1 129 ? -16.731 -27.268 34.428  1.00 42.93  ? 129 MET   A O    1 
ATOM   998  C  CB   . MET   A 1 129 ? -17.579 -24.938 32.876  1.00 48.80  ? 129 MET   A CB   1 
ATOM   999  C  CG   . MET   A 1 129 ? -16.198 -24.326 32.805  1.00 59.50  ? 129 MET   A CG   1 
ATOM   1000 S  SD   . MET   A 1 129 ? -16.196 -22.539 33.131  1.00 85.27  ? 129 MET   A SD   1 
ATOM   1001 C  CE   . MET   A 1 129 ? -16.106 -21.886 31.464  1.00 82.31  ? 129 MET   A CE   1 
ATOM   1002 N  N    . PHE   A 1 130 ? -15.591 -27.758 32.573  1.00 39.04  ? 130 PHE   A N    1 
ATOM   1003 C  CA   . PHE   A 1 130 ? -14.359 -28.281 33.178  1.00 41.84  ? 130 PHE   A CA   1 
ATOM   1004 C  C    . PHE   A 1 130 ? -13.270 -27.285 32.827  1.00 44.71  ? 130 PHE   A C    1 
ATOM   1005 O  O    . PHE   A 1 130 ? -13.097 -27.046 31.623  1.00 42.52  ? 130 PHE   A O    1 
ATOM   1006 C  CB   . PHE   A 1 130 ? -14.025 -29.681 32.638  1.00 46.23  ? 130 PHE   A CB   1 
ATOM   1007 C  CG   . PHE   A 1 130 ? -15.171 -30.657 32.667  1.00 43.65  ? 130 PHE   A CG   1 
ATOM   1008 C  CD1  . PHE   A 1 130 ? -15.450 -31.388 33.814  1.00 49.71  ? 130 PHE   A CD1  1 
ATOM   1009 C  CD2  . PHE   A 1 130 ? -15.974 -30.842 31.551  1.00 47.35  ? 130 PHE   A CD2  1 
ATOM   1010 C  CE1  . PHE   A 1 130 ? -16.520 -32.269 33.849  1.00 54.20  ? 130 PHE   A CE1  1 
ATOM   1011 C  CE2  . PHE   A 1 130 ? -17.033 -31.739 31.578  1.00 51.43  ? 130 PHE   A CE2  1 
ATOM   1012 C  CZ   . PHE   A 1 130 ? -17.321 -32.429 32.736  1.00 55.36  ? 130 PHE   A CZ   1 
ATOM   1013 N  N    . ASN   A 1 131 ? -12.602 -26.733 33.842  1.00 49.52  ? 131 ASN   A N    1 
ATOM   1014 C  CA   . ASN   A 1 131 ? -11.325 -25.989 33.704  1.00 54.82  ? 131 ASN   A CA   1 
ATOM   1015 C  C    . ASN   A 1 131 ? -10.205 -26.851 34.275  1.00 48.64  ? 131 ASN   A C    1 
ATOM   1016 O  O    . ASN   A 1 131 ? -9.121  -26.698 33.808  1.00 59.99  ? 131 ASN   A O    1 
ATOM   1017 C  CB   . ASN   A 1 131 ? -11.355 -24.593 34.335  1.00 56.45  ? 131 ASN   A CB   1 
ATOM   1018 C  CG   . ASN   A 1 131 ? -12.254 -23.625 33.586  1.00 63.22  ? 131 ASN   A CG   1 
ATOM   1019 O  OD1  . ASN   A 1 131 ? -12.033 -23.364 32.409  1.00 69.42  ? 131 ASN   A OD1  1 
ATOM   1020 N  ND2  . ASN   A 1 131 ? -13.276 -23.083 34.241  1.00 63.07  ? 131 ASN   A ND2  1 
ATOM   1021 N  N    . GLN   A 1 132 ? -10.482 -27.707 35.244  1.00 52.29  ? 132 GLN   A N    1 
ATOM   1022 C  CA   . GLN   A 1 132 ? -9.601  -28.829 35.652  1.00 69.69  ? 132 GLN   A CA   1 
ATOM   1023 C  C    . GLN   A 1 132 ? -10.351 -30.139 35.360  1.00 67.94  ? 132 GLN   A C    1 
ATOM   1024 O  O    . GLN   A 1 132 ? -11.595 -30.109 35.329  1.00 76.20  ? 132 GLN   A O    1 
ATOM   1025 C  CB   . GLN   A 1 132 ? -9.200  -28.707 37.129  1.00 79.09  ? 132 GLN   A CB   1 
ATOM   1026 C  CG   . GLN   A 1 132 ? -8.395  -27.452 37.466  1.00 94.99  ? 132 GLN   A CG   1 
ATOM   1027 C  CD   . GLN   A 1 132 ? -7.078  -27.319 36.724  1.00 103.53 ? 132 GLN   A CD   1 
ATOM   1028 O  OE1  . GLN   A 1 132 ? -6.338  -28.281 36.510  1.00 94.41  ? 132 GLN   A OE1  1 
ATOM   1029 N  NE2  . GLN   A 1 132 ? -6.759  -26.095 36.334  1.00 101.41 ? 132 GLN   A NE2  1 
ATOM   1030 N  N    . PHE   A 1 133 ? -9.618  -31.216 35.074  1.00 53.38  ? 133 PHE   A N    1 
ATOM   1031 C  CA   . PHE   A 1 133 ? -10.100 -32.616 35.089  1.00 49.78  ? 133 PHE   A CA   1 
ATOM   1032 C  C    . PHE   A 1 133 ? -9.322  -33.330 36.194  1.00 54.87  ? 133 PHE   A C    1 
ATOM   1033 O  O    . PHE   A 1 133 ? -8.121  -33.077 36.341  1.00 56.19  ? 133 PHE   A O    1 
ATOM   1034 C  CB   . PHE   A 1 133 ? -9.846  -33.336 33.758  1.00 49.44  ? 133 PHE   A CB   1 
ATOM   1035 C  CG   . PHE   A 1 133 ? -10.452 -32.679 32.540  1.00 49.92  ? 133 PHE   A CG   1 
ATOM   1036 C  CD1  . PHE   A 1 133 ? -11.741 -32.969 32.145  1.00 48.46  ? 133 PHE   A CD1  1 
ATOM   1037 C  CD2  . PHE   A 1 133 ? -9.739  -31.753 31.805  1.00 47.83  ? 133 PHE   A CD2  1 
ATOM   1038 C  CE1  . PHE   A 1 133 ? -12.305 -32.332 31.060  1.00 46.73  ? 133 PHE   A CE1  1 
ATOM   1039 C  CE2  . PHE   A 1 133 ? -10.290 -31.154 30.686  1.00 47.15  ? 133 PHE   A CE2  1 
ATOM   1040 C  CZ   . PHE   A 1 133 ? -11.567 -31.448 30.320  1.00 48.67  ? 133 PHE   A CZ   1 
ATOM   1041 N  N    . SER   A 1 134 ? -9.985  -34.216 36.921  1.00 50.40  ? 134 SER   A N    1 
ATOM   1042 C  CA   . SER   A 1 134 ? -9.392  -35.032 37.998  1.00 52.66  ? 134 SER   A CA   1 
ATOM   1043 C  C    . SER   A 1 134 ? -9.284  -36.495 37.565  1.00 54.17  ? 134 SER   A C    1 
ATOM   1044 O  O    . SER   A 1 134 ? -10.017 -36.912 36.617  1.00 56.35  ? 134 SER   A O    1 
ATOM   1045 C  CB   . SER   A 1 134 ? -10.244 -34.895 39.212  1.00 57.21  ? 134 SER   A CB   1 
ATOM   1046 O  OG   . SER   A 1 134 ? -11.613 -34.987 38.845  1.00 65.53  ? 134 SER   A OG   1 
ATOM   1047 N  N    . LYS   A 1 135 ? -8.479  -37.237 38.325  1.00 55.34  ? 135 LYS   A N    1 
ATOM   1048 C  CA   . LYS   A 1 135 ? -8.096  -38.664 38.147  1.00 70.83  ? 135 LYS   A CA   1 
ATOM   1049 C  C    . LYS   A 1 135 ? -9.349  -39.548 38.098  1.00 68.04  ? 135 LYS   A C    1 
ATOM   1050 O  O    . LYS   A 1 135 ? -9.328  -40.606 37.442  1.00 65.78  ? 135 LYS   A O    1 
ATOM   1051 C  CB   . LYS   A 1 135 ? -7.200  -39.119 39.310  1.00 76.77  ? 135 LYS   A CB   1 
ATOM   1052 C  CG   . LYS   A 1 135 ? -5.802  -38.490 39.399  1.00 90.54  ? 135 LYS   A CG   1 
ATOM   1053 C  CD   . LYS   A 1 135 ? -5.727  -36.993 39.767  1.00 101.53 ? 135 LYS   A CD   1 
ATOM   1054 C  CE   . LYS   A 1 135 ? -6.427  -36.600 41.061  1.00 97.60  ? 135 LYS   A CE   1 
ATOM   1055 N  NZ   . LYS   A 1 135 ? -7.088  -35.271 40.964  1.00 89.20  ? 135 LYS   A NZ   1 
ATOM   1056 N  N    . ASP   A 1 136 ? -10.396 -39.155 38.809  1.00 61.87  ? 136 ASP   A N    1 
ATOM   1057 C  CA   . ASP   A 1 136 ? -11.663 -39.914 38.832  1.00 68.29  ? 136 ASP   A CA   1 
ATOM   1058 C  C    . ASP   A 1 136 ? -12.786 -38.946 38.448  1.00 67.56  ? 136 ASP   A C    1 
ATOM   1059 O  O    . ASP   A 1 136 ? -13.375 -38.307 39.360  1.00 68.77  ? 136 ASP   A O    1 
ATOM   1060 C  CB   . ASP   A 1 136 ? -11.809 -40.562 40.203  1.00 84.66  ? 136 ASP   A CB   1 
ATOM   1061 C  CG   . ASP   A 1 136 ? -13.003 -41.483 40.299  1.00 95.90  ? 136 ASP   A CG   1 
ATOM   1062 O  OD1  . ASP   A 1 136 ? -13.206 -42.284 39.341  1.00 88.08  ? 136 ASP   A OD1  1 
ATOM   1063 O  OD2  . ASP   A 1 136 ? -13.722 -41.377 41.324  1.00 97.40  ? 136 ASP   A OD2  1 
ATOM   1064 N  N    . GLN   A 1 137 ? -13.015 -38.782 37.144  1.00 52.78  ? 137 GLN   A N    1 
ATOM   1065 C  CA   . GLN   A 1 137 ? -13.984 -37.796 36.613  1.00 53.71  ? 137 GLN   A CA   1 
ATOM   1066 C  C    . GLN   A 1 137 ? -15.291 -38.521 36.266  1.00 52.04  ? 137 GLN   A C    1 
ATOM   1067 O  O    . GLN   A 1 137 ? -15.501 -38.847 35.090  1.00 53.51  ? 137 GLN   A O    1 
ATOM   1068 C  CB   . GLN   A 1 137 ? -13.354 -37.071 35.434  1.00 58.11  ? 137 GLN   A CB   1 
ATOM   1069 C  CG   . GLN   A 1 137 ? -14.133 -35.852 34.985  1.00 62.40  ? 137 GLN   A CG   1 
ATOM   1070 C  CD   . GLN   A 1 137 ? -13.912 -34.661 35.878  1.00 63.32  ? 137 GLN   A CD   1 
ATOM   1071 O  OE1  . GLN   A 1 137 ? -12.785 -34.334 36.236  1.00 67.21  ? 137 GLN   A OE1  1 
ATOM   1072 N  NE2  . GLN   A 1 137 ? -14.998 -33.986 36.215  1.00 62.12  ? 137 GLN   A NE2  1 
ATOM   1073 N  N    . LYS   A 1 138 ? -16.161 -38.696 37.267  1.00 49.29  ? 138 LYS   A N    1 
ATOM   1074 C  CA   . LYS   A 1 138 ? -17.393 -39.520 37.230  1.00 47.39  ? 138 LYS   A CA   1 
ATOM   1075 C  C    . LYS   A 1 138 ? -18.489 -38.917 36.326  1.00 48.18  ? 138 LYS   A C    1 
ATOM   1076 O  O    . LYS   A 1 138 ? -19.498 -39.598 36.091  1.00 56.89  ? 138 LYS   A O    1 
ATOM   1077 C  CB   . LYS   A 1 138 ? -17.873 -39.708 38.674  1.00 47.51  ? 138 LYS   A CB   1 
ATOM   1078 C  CG   . LYS   A 1 138 ? -17.109 -40.761 39.456  1.00 46.93  ? 138 LYS   A CG   1 
ATOM   1079 C  CD   . LYS   A 1 138 ? -17.645 -40.950 40.849  1.00 57.29  ? 138 LYS   A CD   1 
ATOM   1080 C  CE   . LYS   A 1 138 ? -16.712 -41.656 41.809  1.00 59.61  ? 138 LYS   A CE   1 
ATOM   1081 N  NZ   . LYS   A 1 138 ? -16.351 -43.013 41.313  1.00 69.85  ? 138 LYS   A NZ   1 
ATOM   1082 N  N    . ASP   A 1 139 ? -18.358 -37.680 35.853  1.00 47.41  ? 139 ASP   A N    1 
ATOM   1083 C  CA   . ASP   A 1 139 ? -19.322 -37.100 34.879  1.00 44.98  ? 139 ASP   A CA   1 
ATOM   1084 C  C    . ASP   A 1 139 ? -18.742 -37.191 33.457  1.00 39.13  ? 139 ASP   A C    1 
ATOM   1085 O  O    . ASP   A 1 139 ? -19.385 -36.690 32.536  1.00 38.67  ? 139 ASP   A O    1 
ATOM   1086 C  CB   . ASP   A 1 139 ? -19.764 -35.691 35.295  1.00 41.52  ? 139 ASP   A CB   1 
ATOM   1087 C  CG   . ASP   A 1 139 ? -18.606 -34.743 35.504  1.00 46.61  ? 139 ASP   A CG   1 
ATOM   1088 O  OD1  . ASP   A 1 139 ? -17.472 -35.242 35.484  1.00 51.49  ? 139 ASP   A OD1  1 
ATOM   1089 O  OD2  . ASP   A 1 139 ? -18.843 -33.520 35.711  1.00 47.10  ? 139 ASP   A OD2  1 
ATOM   1090 N  N    . LEU   A 1 140 ? -17.585 -37.816 33.268  1.00 37.24  ? 140 LEU   A N    1 
ATOM   1091 C  CA   . LEU   A 1 140 ? -17.100 -38.190 31.910  1.00 43.01  ? 140 LEU   A CA   1 
ATOM   1092 C  C    . LEU   A 1 140 ? -17.149 -39.709 31.703  1.00 46.76  ? 140 LEU   A C    1 
ATOM   1093 O  O    . LEU   A 1 140 ? -16.865 -40.457 32.666  1.00 51.60  ? 140 LEU   A O    1 
ATOM   1094 C  CB   . LEU   A 1 140 ? -15.674 -37.698 31.728  1.00 39.52  ? 140 LEU   A CB   1 
ATOM   1095 C  CG   . LEU   A 1 140 ? -15.548 -36.199 31.630  1.00 38.98  ? 140 LEU   A CG   1 
ATOM   1096 C  CD1  . LEU   A 1 140 ? -14.126 -35.840 31.302  1.00 42.89  ? 140 LEU   A CD1  1 
ATOM   1097 C  CD2  . LEU   A 1 140 ? -16.523 -35.642 30.607  1.00 43.28  ? 140 LEU   A CD2  1 
ATOM   1098 N  N    . ILE   A 1 141 ? -17.506 -40.119 30.485  1.00 40.15  ? 141 ILE   A N    1 
ATOM   1099 C  CA   . ILE   A 1 141 ? -17.383 -41.513 29.989  1.00 44.43  ? 141 ILE   A CA   1 
ATOM   1100 C  C    . ILE   A 1 141 ? -16.105 -41.505 29.148  1.00 51.84  ? 141 ILE   A C    1 
ATOM   1101 O  O    . ILE   A 1 141 ? -16.124 -40.832 28.078  1.00 45.55  ? 141 ILE   A O    1 
ATOM   1102 C  CB   . ILE   A 1 141 ? -18.627 -41.951 29.179  1.00 48.89  ? 141 ILE   A CB   1 
ATOM   1103 C  CG1  . ILE   A 1 141 ? -19.927 -41.861 29.988  1.00 49.04  ? 141 ILE   A CG1  1 
ATOM   1104 C  CG2  . ILE   A 1 141 ? -18.453 -43.341 28.587  1.00 48.29  ? 141 ILE   A CG2  1 
ATOM   1105 C  CD1  . ILE   A 1 141 ? -21.175 -41.962 29.127  1.00 49.04  ? 141 ILE   A CD1  1 
ATOM   1106 N  N    . LEU   A 1 142 ? -15.039 -42.150 29.652  1.00 46.44  ? 142 LEU   A N    1 
ATOM   1107 C  CA   . LEU   A 1 142 ? -13.756 -42.323 28.933  1.00 44.43  ? 142 LEU   A CA   1 
ATOM   1108 C  C    . LEU   A 1 142 ? -13.813 -43.642 28.168  1.00 46.69  ? 142 LEU   A C    1 
ATOM   1109 O  O    . LEU   A 1 142 ? -14.337 -44.615 28.716  1.00 45.38  ? 142 LEU   A O    1 
ATOM   1110 C  CB   . LEU   A 1 142 ? -12.590 -42.297 29.920  1.00 43.73  ? 142 LEU   A CB   1 
ATOM   1111 C  CG   . LEU   A 1 142 ? -12.457 -41.020 30.750  1.00 41.10  ? 142 LEU   A CG   1 
ATOM   1112 C  CD1  . LEU   A 1 142 ? -11.199 -41.069 31.578  1.00 38.88  ? 142 LEU   A CD1  1 
ATOM   1113 C  CD2  . LEU   A 1 142 ? -12.461 -39.781 29.881  1.00 41.74  ? 142 LEU   A CD2  1 
ATOM   1114 N  N    . GLN   A 1 143 ? -13.393 -43.592 26.909  1.00 45.11  ? 143 GLN   A N    1 
ATOM   1115 C  CA   . GLN   A 1 143 ? -13.395 -44.711 25.945  1.00 44.73  ? 143 GLN   A CA   1 
ATOM   1116 C  C    . GLN   A 1 143 ? -12.020 -44.768 25.253  1.00 43.77  ? 143 GLN   A C    1 
ATOM   1117 O  O    . GLN   A 1 143 ? -11.355 -43.703 25.081  1.00 40.09  ? 143 GLN   A O    1 
ATOM   1118 C  CB   . GLN   A 1 143 ? -14.503 -44.537 24.901  1.00 45.37  ? 143 GLN   A CB   1 
ATOM   1119 C  CG   . GLN   A 1 143 ? -15.885 -44.196 25.447  1.00 44.53  ? 143 GLN   A CG   1 
ATOM   1120 C  CD   . GLN   A 1 143 ? -16.887 -44.114 24.317  1.00 44.72  ? 143 GLN   A CD   1 
ATOM   1121 O  OE1  . GLN   A 1 143 ? -16.580 -43.659 23.209  1.00 44.50  ? 143 GLN   A OE1  1 
ATOM   1122 N  NE2  . GLN   A 1 143 ? -18.091 -44.599 24.563  1.00 34.90  ? 143 GLN   A NE2  1 
ATOM   1123 N  N    . GLY   A 1 144 ? -11.603 -45.968 24.853  1.00 43.77  ? 144 GLY   A N    1 
ATOM   1124 C  CA   . GLY   A 1 144 ? -10.313 -46.169 24.179  1.00 46.92  ? 144 GLY   A CA   1 
ATOM   1125 C  C    . GLY   A 1 144 ? -9.186  -45.768 25.108  1.00 45.27  ? 144 GLY   A C    1 
ATOM   1126 O  O    . GLY   A 1 144 ? -9.235  -46.200 26.236  1.00 41.81  ? 144 GLY   A O    1 
ATOM   1127 N  N    . ASP   A 1 145 ? -8.238  -44.942 24.652  1.00 44.38  ? 145 ASP   A N    1 
ATOM   1128 C  CA   . ASP   A 1 145 ? -6.969  -44.680 25.377  1.00 42.86  ? 145 ASP   A CA   1 
ATOM   1129 C  C    . ASP   A 1 145 ? -7.107  -43.459 26.295  1.00 44.68  ? 145 ASP   A C    1 
ATOM   1130 O  O    . ASP   A 1 145 ? -6.110  -43.142 26.986  1.00 48.07  ? 145 ASP   A O    1 
ATOM   1131 C  CB   . ASP   A 1 145 ? -5.820  -44.475 24.376  1.00 45.78  ? 145 ASP   A CB   1 
ATOM   1132 C  CG   . ASP   A 1 145 ? -5.496  -45.718 23.554  1.00 48.71  ? 145 ASP   A CG   1 
ATOM   1133 O  OD1  . ASP   A 1 145 ? -5.626  -46.812 24.124  1.00 54.95  ? 145 ASP   A OD1  1 
ATOM   1134 O  OD2  . ASP   A 1 145 ? -5.099  -45.590 22.355  1.00 44.99  ? 145 ASP   A OD2  1 
ATOM   1135 N  N    . ALA   A 1 146 ? -8.272  -42.793 26.327  1.00 43.02  ? 146 ALA   A N    1 
ATOM   1136 C  CA   . ALA   A 1 146 ? -8.458  -41.475 26.999  1.00 42.88  ? 146 ALA   A CA   1 
ATOM   1137 C  C    . ALA   A 1 146 ? -8.210  -41.605 28.504  1.00 42.68  ? 146 ALA   A C    1 
ATOM   1138 O  O    . ALA   A 1 146 ? -8.674  -42.608 29.084  1.00 45.71  ? 146 ALA   A O    1 
ATOM   1139 C  CB   . ALA   A 1 146 ? -9.829  -40.918 26.703  1.00 44.02  ? 146 ALA   A CB   1 
ATOM   1140 N  N    . THR   A 1 147 ? -7.510  -40.632 29.085  1.00 44.27  ? 147 THR   A N    1 
ATOM   1141 C  CA   . THR   A 1 147 ? -7.215  -40.613 30.538  1.00 50.79  ? 147 THR   A CA   1 
ATOM   1142 C  C    . THR   A 1 147 ? -7.324  -39.186 31.070  1.00 51.46  ? 147 THR   A C    1 
ATOM   1143 O  O    . THR   A 1 147 ? -7.272  -38.257 30.277  1.00 47.23  ? 147 THR   A O    1 
ATOM   1144 C  CB   . THR   A 1 147 ? -5.828  -41.172 30.865  1.00 56.22  ? 147 THR   A CB   1 
ATOM   1145 O  OG1  . THR   A 1 147 ? -4.860  -40.443 30.121  1.00 58.61  ? 147 THR   A OG1  1 
ATOM   1146 C  CG2  . THR   A 1 147 ? -5.682  -42.641 30.555  1.00 55.32  ? 147 THR   A CG2  1 
ATOM   1147 N  N    . THR   A 1 148 ? -7.473  -39.059 32.385  1.00 58.08  ? 148 THR   A N    1 
ATOM   1148 C  CA   . THR   A 1 148 ? -7.564  -37.750 33.072  1.00 64.29  ? 148 THR   A CA   1 
ATOM   1149 C  C    . THR   A 1 148 ? -6.646  -37.760 34.290  1.00 63.75  ? 148 THR   A C    1 
ATOM   1150 O  O    . THR   A 1 148 ? -6.264  -38.839 34.725  1.00 61.65  ? 148 THR   A O    1 
ATOM   1151 C  CB   . THR   A 1 148 ? -8.954  -37.481 33.652  1.00 57.59  ? 148 THR   A CB   1 
ATOM   1152 O  OG1  . THR   A 1 148 ? -9.347  -38.653 34.353  1.00 69.36  ? 148 THR   A OG1  1 
ATOM   1153 C  CG2  . THR   A 1 148 ? -9.996  -37.128 32.623  1.00 58.21  ? 148 THR   A CG2  1 
ATOM   1154 N  N    . GLY   A 1 149 ? -6.321  -36.573 34.794  1.00 73.54  ? 149 GLY   A N    1 
ATOM   1155 C  CA   . GLY   A 1 149 ? -5.516  -36.406 36.014  1.00 87.36  ? 149 GLY   A CA   1 
ATOM   1156 C  C    . GLY   A 1 149 ? -4.061  -36.085 35.764  1.00 90.45  ? 149 GLY   A C    1 
ATOM   1157 O  O    . GLY   A 1 149 ? -3.421  -35.590 36.689  1.00 101.15 ? 149 GLY   A O    1 
ATOM   1158 N  N    . THR   A 1 150 ? -3.558  -36.279 34.554  1.00 89.32  ? 150 THR   A N    1 
ATOM   1159 C  CA   . THR   A 1 150 ? -2.137  -35.918 34.356  1.00 93.55  ? 150 THR   A CA   1 
ATOM   1160 C  C    . THR   A 1 150 ? -2.139  -34.411 34.105  1.00 88.81  ? 150 THR   A C    1 
ATOM   1161 O  O    . THR   A 1 150 ? -2.603  -34.030 33.036  1.00 87.32  ? 150 THR   A O    1 
ATOM   1162 C  CB   . THR   A 1 150 ? -1.550  -36.766 33.223  1.00 102.05 ? 150 THR   A CB   1 
ATOM   1163 O  OG1  . THR   A 1 150 ? -1.073  -37.983 33.793  1.00 91.36  ? 150 THR   A OG1  1 
ATOM   1164 C  CG2  . THR   A 1 150 ? -0.450  -36.077 32.447  1.00 96.66  ? 150 THR   A CG2  1 
ATOM   1165 N  N    . ASP   A 1 151 ? -1.696  -33.631 35.101  1.00 76.53  ? 151 ASP   A N    1 
ATOM   1166 C  CA   . ASP   A 1 151 ? -1.653  -32.140 35.146  1.00 81.59  ? 151 ASP   A CA   1 
ATOM   1167 C  C    . ASP   A 1 151 ? -3.067  -31.557 35.148  1.00 70.22  ? 151 ASP   A C    1 
ATOM   1168 O  O    . ASP   A 1 151 ? -3.209  -30.409 34.737  1.00 70.52  ? 151 ASP   A O    1 
ATOM   1169 C  CB   . ASP   A 1 151 ? -0.925  -31.484 33.967  1.00 90.32  ? 151 ASP   A CB   1 
ATOM   1170 C  CG   . ASP   A 1 151 ? 0.547   -31.804 33.822  1.00 94.24  ? 151 ASP   A CG   1 
ATOM   1171 O  OD1  . ASP   A 1 151 ? 1.006   -32.766 34.447  1.00 103.59 ? 151 ASP   A OD1  1 
ATOM   1172 O  OD2  . ASP   A 1 151 ? 1.216   -31.079 33.072  1.00 96.22  ? 151 ASP   A OD2  1 
ATOM   1173 N  N    . GLY   A 1 152 ? -4.067  -32.298 35.619  1.00 57.36  ? 152 GLY   A N    1 
ATOM   1174 C  CA   . GLY   A 1 152 ? -5.465  -31.831 35.561  1.00 59.07  ? 152 GLY   A CA   1 
ATOM   1175 C  C    . GLY   A 1 152 ? -5.937  -31.632 34.130  1.00 56.73  ? 152 GLY   A C    1 
ATOM   1176 O  O    . GLY   A 1 152 ? -6.756  -30.757 33.898  1.00 59.29  ? 152 GLY   A O    1 
ATOM   1177 N  N    . ASN   A 1 153 ? -5.483  -32.480 33.215  1.00 50.32  ? 153 ASN   A N    1 
ATOM   1178 C  CA   . ASN   A 1 153 ? -5.796  -32.356 31.777  1.00 48.52  ? 153 ASN   A CA   1 
ATOM   1179 C  C    . ASN   A 1 153 ? -6.376  -33.673 31.290  1.00 44.62  ? 153 ASN   A C    1 
ATOM   1180 O  O    . ASN   A 1 153 ? -6.141  -34.678 31.922  1.00 45.33  ? 153 ASN   A O    1 
ATOM   1181 C  CB   . ASN   A 1 153 ? -4.526  -32.138 30.962  1.00 50.97  ? 153 ASN   A CB   1 
ATOM   1182 C  CG   . ASN   A 1 153 ? -3.937  -30.755 31.086  1.00 53.83  ? 153 ASN   A CG   1 
ATOM   1183 O  OD1  . ASN   A 1 153 ? -4.647  -29.783 31.276  1.00 59.38  ? 153 ASN   A OD1  1 
ATOM   1184 N  ND2  . ASN   A 1 153 ? -2.633  -30.659 30.953  1.00 49.29  ? 153 ASN   A ND2  1 
ATOM   1185 N  N    . LEU   A 1 154 ? -7.136  -33.626 30.211  1.00 42.39  ? 154 LEU   A N    1 
ATOM   1186 C  CA   . LEU   A 1 154 ? -7.700  -34.857 29.630  1.00 46.19  ? 154 LEU   A CA   1 
ATOM   1187 C  C    . LEU   A 1 154 ? -6.792  -35.249 28.468  1.00 48.16  ? 154 LEU   A C    1 
ATOM   1188 O  O    . LEU   A 1 154 ? -6.616  -34.446 27.583  1.00 46.84  ? 154 LEU   A O    1 
ATOM   1189 C  CB   . LEU   A 1 154 ? -9.128  -34.551 29.182  1.00 41.18  ? 154 LEU   A CB   1 
ATOM   1190 C  CG   . LEU   A 1 154 ? -9.734  -35.482 28.142  1.00 42.87  ? 154 LEU   A CG   1 
ATOM   1191 C  CD1  . LEU   A 1 154 ? -9.896  -36.878 28.686  1.00 42.41  ? 154 LEU   A CD1  1 
ATOM   1192 C  CD2  . LEU   A 1 154 ? -11.073 -34.949 27.693  1.00 45.51  ? 154 LEU   A CD2  1 
ATOM   1193 N  N    . GLU   A 1 155 ? -6.157  -36.410 28.555  1.00 48.59  ? 155 GLU   A N    1 
ATOM   1194 C  CA   . GLU   A 1 155 ? -5.282  -36.900 27.457  1.00 50.37  ? 155 GLU   A CA   1 
ATOM   1195 C  C    . GLU   A 1 155 ? -6.139  -37.836 26.597  1.00 44.88  ? 155 GLU   A C    1 
ATOM   1196 O  O    . GLU   A 1 155 ? -6.543  -38.901 27.093  1.00 50.22  ? 155 GLU   A O    1 
ATOM   1197 C  CB   . GLU   A 1 155 ? -4.006  -37.572 27.990  1.00 50.04  ? 155 GLU   A CB   1 
ATOM   1198 C  CG   . GLU   A 1 155 ? -2.954  -36.608 28.506  1.00 53.86  ? 155 GLU   A CG   1 
ATOM   1199 C  CD   . GLU   A 1 155 ? -2.269  -35.656 27.526  1.00 61.29  ? 155 GLU   A CD   1 
ATOM   1200 O  OE1  . GLU   A 1 155 ? -2.576  -35.660 26.288  1.00 66.25  ? 155 GLU   A OE1  1 
ATOM   1201 O  OE2  . GLU   A 1 155 ? -1.407  -34.899 28.010  1.00 65.84  ? 155 GLU   A OE2  1 
ATOM   1202 N  N    . LEU   A 1 156 ? -6.507  -37.420 25.392  1.00 44.94  ? 156 LEU   A N    1 
ATOM   1203 C  CA   . LEU   A 1 156 ? -7.433  -38.228 24.558  1.00 44.33  ? 156 LEU   A CA   1 
ATOM   1204 C  C    . LEU   A 1 156 ? -6.684  -39.454 24.009  1.00 44.40  ? 156 LEU   A C    1 
ATOM   1205 O  O    . LEU   A 1 156 ? -7.287  -40.537 23.942  1.00 48.52  ? 156 LEU   A O    1 
ATOM   1206 C  CB   . LEU   A 1 156 ? -8.016  -37.341 23.461  1.00 44.48  ? 156 LEU   A CB   1 
ATOM   1207 C  CG   . LEU   A 1 156 ? -9.116  -36.373 23.903  1.00 41.54  ? 156 LEU   A CG   1 
ATOM   1208 C  CD1  . LEU   A 1 156 ? -9.555  -35.530 22.732  1.00 44.95  ? 156 LEU   A CD1  1 
ATOM   1209 C  CD2  . LEU   A 1 156 ? -10.316 -37.080 24.505  1.00 39.87  ? 156 LEU   A CD2  1 
ATOM   1210 N  N    . THR   A 1 157 ? -5.395  -39.317 23.698  1.00 44.79  ? 157 THR   A N    1 
ATOM   1211 C  CA   . THR   A 1 157 ? -4.563  -40.414 23.157  1.00 43.32  ? 157 THR   A CA   1 
ATOM   1212 C  C    . THR   A 1 157 ? -3.347  -40.638 24.062  1.00 43.29  ? 157 THR   A C    1 
ATOM   1213 O  O    . THR   A 1 157 ? -2.942  -39.726 24.783  1.00 46.68  ? 157 THR   A O    1 
ATOM   1214 C  CB   . THR   A 1 157 ? -4.215  -40.172 21.683  1.00 42.14  ? 157 THR   A CB   1 
ATOM   1215 O  OG1  . THR   A 1 157 ? -3.635  -38.872 21.548  1.00 43.13  ? 157 THR   A OG1  1 
ATOM   1216 C  CG2  . THR   A 1 157 ? -5.402  -40.324 20.758  1.00 44.11  ? 157 THR   A CG2  1 
ATOM   1217 N  N    . ARG   A 1 158 ? -2.805  -41.848 23.970  1.00 51.04  ? 158 ARG   A N    1 
ATOM   1218 C  CA   . ARG   A 1 158 ? -1.757  -42.441 24.842  1.00 57.06  ? 158 ARG   A CA   1 
ATOM   1219 C  C    . ARG   A 1 158 ? -0.480  -41.611 24.758  1.00 56.86  ? 158 ARG   A C    1 
ATOM   1220 O  O    . ARG   A 1 158 ? 0.053   -41.421 23.633  1.00 58.05  ? 158 ARG   A O    1 
ATOM   1221 C  CB   . ARG   A 1 158 ? -1.515  -43.884 24.403  1.00 62.91  ? 158 ARG   A CB   1 
ATOM   1222 C  CG   . ARG   A 1 158 ? -0.940  -44.813 25.465  1.00 79.11  ? 158 ARG   A CG   1 
ATOM   1223 C  CD   . ARG   A 1 158 ? -1.626  -46.150 25.252  1.00 91.96  ? 158 ARG   A CD   1 
ATOM   1224 N  NE   . ARG   A 1 158 ? -0.770  -47.322 25.257  1.00 100.86 ? 158 ARG   A NE   1 
ATOM   1225 C  CZ   . ARG   A 1 158 ? -0.986  -48.403 24.506  1.00 112.03 ? 158 ARG   A CZ   1 
ATOM   1226 N  NH1  . ARG   A 1 158 ? -2.009  -48.442 23.666  1.00 114.82 ? 158 ARG   A NH1  1 
ATOM   1227 N  NH2  . ARG   A 1 158 ? -0.177  -49.445 24.588  1.00 116.62 ? 158 ARG   A NH2  1 
ATOM   1228 N  N    . VAL   A 1 159 ? -0.028  -41.135 25.914  1.00 59.63  ? 159 VAL   A N    1 
ATOM   1229 C  CA   . VAL   A 1 159 ? 1.277   -40.442 26.087  1.00 64.37  ? 159 VAL   A CA   1 
ATOM   1230 C  C    . VAL   A 1 159 ? 2.099   -41.227 27.117  1.00 66.89  ? 159 VAL   A C    1 
ATOM   1231 O  O    . VAL   A 1 159 ? 1.532   -41.700 28.105  1.00 62.39  ? 159 VAL   A O    1 
ATOM   1232 C  CB   . VAL   A 1 159 ? 1.063   -38.967 26.479  1.00 66.21  ? 159 VAL   A CB   1 
ATOM   1233 C  CG1  . VAL   A 1 159 ? 2.382   -38.207 26.577  1.00 72.98  ? 159 VAL   A CG1  1 
ATOM   1234 C  CG2  . VAL   A 1 159 ? 0.137   -38.258 25.499  1.00 61.05  ? 159 VAL   A CG2  1 
ATOM   1235 N  N    . SER   A 1 160 ? 3.399   -41.385 26.881  1.00 72.81  ? 160 SER   A N    1 
ATOM   1236 C  CA   . SER   A 1 160 ? 4.338   -41.983 27.869  1.00 76.75  ? 160 SER   A CA   1 
ATOM   1237 C  C    . SER   A 1 160 ? 4.477   -41.022 29.065  1.00 75.04  ? 160 SER   A C    1 
ATOM   1238 O  O    . SER   A 1 160 ? 4.016   -39.863 28.952  1.00 69.12  ? 160 SER   A O    1 
ATOM   1239 C  CB   . SER   A 1 160 ? 5.672   -42.318 27.218  1.00 74.69  ? 160 SER   A CB   1 
ATOM   1240 O  OG   . SER   A 1 160 ? 6.427   -41.141 26.944  1.00 69.05  ? 160 SER   A OG   1 
ATOM   1241 N  N    . SER   A 1 161 ? 5.096   -41.472 30.161  1.00 80.44  ? 161 SER   A N    1 
ATOM   1242 C  CA   . SER   A 1 161 ? 5.398   -40.656 31.375  1.00 83.29  ? 161 SER   A CA   1 
ATOM   1243 C  C    . SER   A 1 161 ? 6.311   -39.452 31.048  1.00 79.63  ? 161 SER   A C    1 
ATOM   1244 O  O    . SER   A 1 161 ? 6.052   -38.369 31.567  1.00 78.46  ? 161 SER   A O    1 
ATOM   1245 C  CB   . SER   A 1 161 ? 5.954   -41.515 32.502  1.00 82.71  ? 161 SER   A CB   1 
ATOM   1246 O  OG   . SER   A 1 161 ? 6.984   -42.381 32.050  1.00 79.61  ? 161 SER   A OG   1 
ATOM   1247 N  N    . ASN   A 1 162 ? 7.329   -39.588 30.198  1.00 86.90  ? 162 ASN   A N    1 
ATOM   1248 C  CA   . ASN   A 1 162 ? 8.230   -38.445 29.879  1.00 85.65  ? 162 ASN   A CA   1 
ATOM   1249 C  C    . ASN   A 1 162 ? 7.470   -37.422 29.018  1.00 89.97  ? 162 ASN   A C    1 
ATOM   1250 O  O    . ASN   A 1 162 ? 7.879   -36.251 29.018  1.00 94.97  ? 162 ASN   A O    1 
ATOM   1251 C  CB   . ASN   A 1 162 ? 9.553   -38.908 29.264  1.00 87.30  ? 162 ASN   A CB   1 
ATOM   1252 C  CG   . ASN   A 1 162 ? 9.383   -40.004 28.239  1.00 87.65  ? 162 ASN   A CG   1 
ATOM   1253 O  OD1  . ASN   A 1 162 ? 9.115   -39.729 27.077  1.00 94.31  ? 162 ASN   A OD1  1 
ATOM   1254 N  ND2  . ASN   A 1 162 ? 9.546   -41.247 28.659  1.00 82.65  ? 162 ASN   A ND2  1 
ATOM   1255 N  N    . GLY   A 1 163 ? 6.393   -37.835 28.341  1.00 86.78  ? 163 GLY   A N    1 
ATOM   1256 C  CA   . GLY   A 1 163 ? 5.515   -36.954 27.542  1.00 84.12  ? 163 GLY   A CA   1 
ATOM   1257 C  C    . GLY   A 1 163 ? 5.528   -37.270 26.041  1.00 86.98  ? 163 GLY   A C    1 
ATOM   1258 O  O    . GLY   A 1 163 ? 5.128   -36.377 25.247  1.00 77.72  ? 163 GLY   A O    1 
ATOM   1259 N  N    . SER   A 1 164 ? 5.918   -38.491 25.635  1.00 76.84  ? 164 SER   A N    1 
ATOM   1260 C  CA   . SER   A 1 164 ? 5.990   -38.914 24.207  1.00 73.81  ? 164 SER   A CA   1 
ATOM   1261 C  C    . SER   A 1 164 ? 4.682   -39.557 23.727  1.00 61.37  ? 164 SER   A C    1 
ATOM   1262 O  O    . SER   A 1 164 ? 4.187   -40.539 24.279  1.00 47.90  ? 164 SER   A O    1 
ATOM   1263 C  CB   . SER   A 1 164 ? 7.166   -39.808 23.946  1.00 73.88  ? 164 SER   A CB   1 
ATOM   1264 O  OG   . SER   A 1 164 ? 8.362   -39.053 23.984  1.00 77.53  ? 164 SER   A OG   1 
ATOM   1265 N  N    . PRO   A 1 165 ? 4.063   -38.986 22.677  1.00 51.14  ? 165 PRO   A N    1 
ATOM   1266 C  CA   . PRO   A 1 165 ? 2.813   -39.521 22.143  1.00 52.55  ? 165 PRO   A CA   1 
ATOM   1267 C  C    . PRO   A 1 165 ? 3.030   -40.811 21.352  1.00 48.49  ? 165 PRO   A C    1 
ATOM   1268 O  O    . PRO   A 1 165 ? 4.007   -40.939 20.682  1.00 57.14  ? 165 PRO   A O    1 
ATOM   1269 C  CB   . PRO   A 1 165 ? 2.286   -38.384 21.255  1.00 53.55  ? 165 PRO   A CB   1 
ATOM   1270 C  CG   . PRO   A 1 165 ? 3.537   -37.629 20.823  1.00 53.93  ? 165 PRO   A CG   1 
ATOM   1271 C  CD   . PRO   A 1 165 ? 4.486   -37.751 22.002  1.00 54.27  ? 165 PRO   A CD   1 
ATOM   1272 N  N    . GLN   A 1 166 ? 2.091   -41.736 21.476  1.00 49.26  ? 166 GLN   A N    1 
ATOM   1273 C  CA   . GLN   A 1 166 ? 2.107   -43.046 20.789  1.00 47.02  ? 166 GLN   A CA   1 
ATOM   1274 C  C    . GLN   A 1 166 ? 1.193   -42.991 19.549  1.00 50.42  ? 166 GLN   A C    1 
ATOM   1275 O  O    . GLN   A 1 166 ? 0.201   -42.165 19.505  1.00 45.08  ? 166 GLN   A O    1 
ATOM   1276 C  CB   . GLN   A 1 166 ? 1.691   -44.140 21.781  1.00 56.64  ? 166 GLN   A CB   1 
ATOM   1277 C  CG   . GLN   A 1 166 ? 2.822   -44.648 22.677  1.00 65.11  ? 166 GLN   A CG   1 
ATOM   1278 C  CD   . GLN   A 1 166 ? 3.439   -45.952 22.206  1.00 73.93  ? 166 GLN   A CD   1 
ATOM   1279 O  OE1  . GLN   A 1 166 ? 4.618   -45.985 21.886  1.00 74.14  ? 166 GLN   A OE1  1 
ATOM   1280 N  NE2  . GLN   A 1 166 ? 2.673   -47.042 22.173  1.00 67.15  ? 166 GLN   A NE2  1 
ATOM   1281 N  N    . GLY   A 1 167 ? 1.570   -43.802 18.552  1.00 48.38  ? 167 GLY   A N    1 
ATOM   1282 C  CA   . GLY   A 1 167 ? 0.900   -44.003 17.255  1.00 44.84  ? 167 GLY   A CA   1 
ATOM   1283 C  C    . GLY   A 1 167 ? -0.156  -45.066 17.424  1.00 43.18  ? 167 GLY   A C    1 
ATOM   1284 O  O    . GLY   A 1 167 ? -0.173  -45.666 18.481  1.00 43.18  ? 167 GLY   A O    1 
ATOM   1285 N  N    . SER   A 1 168 ? -1.086  -45.201 16.483  1.00 45.17  ? 168 SER   A N    1 
ATOM   1286 C  CA   . SER   A 1 168 ? -2.156  -46.232 16.529  1.00 46.43  ? 168 SER   A CA   1 
ATOM   1287 C  C    . SER   A 1 168 ? -2.946  -46.109 17.844  1.00 43.02  ? 168 SER   A C    1 
ATOM   1288 O  O    . SER   A 1 168 ? -3.546  -47.087 18.249  1.00 38.76  ? 168 SER   A O    1 
ATOM   1289 C  CB   . SER   A 1 168 ? -1.558  -47.602 16.314  1.00 40.82  ? 168 SER   A CB   1 
ATOM   1290 O  OG   . SER   A 1 168 ? -0.650  -47.541 15.223  1.00 50.99  ? 168 SER   A OG   1 
ATOM   1291 N  N    . SER   A 1 169 ? -3.046  -44.898 18.404  1.00 43.77  ? 169 SER   A N    1 
ATOM   1292 C  CA   . SER   A 1 169 ? -3.916  -44.572 19.563  1.00 41.37  ? 169 SER   A CA   1 
ATOM   1293 C  C    . SER   A 1 169 ? -5.251  -43.959 19.101  1.00 46.96  ? 169 SER   A C    1 
ATOM   1294 O  O    . SER   A 1 169 ? -5.267  -43.218 18.081  1.00 44.37  ? 169 SER   A O    1 
ATOM   1295 C  CB   . SER   A 1 169 ? -3.213  -43.645 20.488  1.00 40.99  ? 169 SER   A CB   1 
ATOM   1296 O  OG   . SER   A 1 169 ? -3.934  -43.553 21.700  1.00 44.93  ? 169 SER   A OG   1 
ATOM   1297 N  N    . VAL   A 1 170 ? -6.327  -44.233 19.852  1.00 42.37  ? 170 VAL   A N    1 
ATOM   1298 C  CA   . VAL   A 1 170 ? -7.653  -43.583 19.683  1.00 42.10  ? 170 VAL   A CA   1 
ATOM   1299 C  C    . VAL   A 1 170 ? -8.296  -43.425 21.061  1.00 44.24  ? 170 VAL   A C    1 
ATOM   1300 O  O    . VAL   A 1 170 ? -8.050  -44.264 21.984  1.00 41.68  ? 170 VAL   A O    1 
ATOM   1301 C  CB   . VAL   A 1 170 ? -8.546  -44.346 18.681  1.00 46.73  ? 170 VAL   A CB   1 
ATOM   1302 C  CG1  . VAL   A 1 170 ? -8.874  -45.769 19.125  1.00 46.67  ? 170 VAL   A CG1  1 
ATOM   1303 C  CG2  . VAL   A 1 170 ? -9.806  -43.572 18.355  1.00 42.30  ? 170 VAL   A CG2  1 
ATOM   1304 N  N    . GLY   A 1 171 ? -9.052  -42.338 21.235  1.00 46.37  ? 171 GLY   A N    1 
ATOM   1305 C  CA   . GLY   A 1 171 ? -9.585  -42.005 22.560  1.00 44.49  ? 171 GLY   A CA   1 
ATOM   1306 C  C    . GLY   A 1 171 ? -10.723 -41.037 22.489  1.00 44.97  ? 171 GLY   A C    1 
ATOM   1307 O  O    . GLY   A 1 171 ? -10.678 -40.161 21.631  1.00 44.77  ? 171 GLY   A O    1 
ATOM   1308 N  N    . ARG   A 1 172 ? -11.678 -41.157 23.410  1.00 39.91  ? 172 ARG   A N    1 
ATOM   1309 C  CA   . ARG   A 1 172 ? -12.786 -40.192 23.478  1.00 40.64  ? 172 ARG   A CA   1 
ATOM   1310 C  C    . ARG   A 1 172 ? -13.158 -39.918 24.935  1.00 45.25  ? 172 ARG   A C    1 
ATOM   1311 O  O    . ARG   A 1 172 ? -12.860 -40.759 25.810  1.00 48.58  ? 172 ARG   A O    1 
ATOM   1312 C  CB   . ARG   A 1 172 ? -13.964 -40.722 22.646  1.00 36.63  ? 172 ARG   A CB   1 
ATOM   1313 C  CG   . ARG   A 1 172 ? -13.548 -41.204 21.274  1.00 35.24  ? 172 ARG   A CG   1 
ATOM   1314 C  CD   . ARG   A 1 172 ? -14.630 -41.606 20.284  1.00 39.08  ? 172 ARG   A CD   1 
ATOM   1315 N  NE   . ARG   A 1 172 ? -15.892 -42.092 20.792  1.00 38.68  ? 172 ARG   A NE   1 
ATOM   1316 C  CZ   . ARG   A 1 172 ? -16.961 -42.320 20.036  1.00 40.23  ? 172 ARG   A CZ   1 
ATOM   1317 N  NH1  . ARG   A 1 172 ? -16.908 -42.125 18.724  1.00 39.74  ? 172 ARG   A NH1  1 
ATOM   1318 N  NH2  . ARG   A 1 172 ? -18.075 -42.761 20.603  1.00 36.95  ? 172 ARG   A NH2  1 
ATOM   1319 N  N    . ALA   A 1 173 ? -13.834 -38.786 25.165  1.00 45.09  ? 173 ALA   A N    1 
ATOM   1320 C  CA   . ALA   A 1 173 ? -14.495 -38.444 26.441  1.00 41.98  ? 173 ALA   A CA   1 
ATOM   1321 C  C    . ALA   A 1 173 ? -15.868 -37.877 26.111  1.00 41.92  ? 173 ALA   A C    1 
ATOM   1322 O  O    . ALA   A 1 173 ? -15.918 -37.049 25.195  1.00 38.04  ? 173 ALA   A O    1 
ATOM   1323 C  CB   . ALA   A 1 173 ? -13.642 -37.467 27.196  1.00 46.87  ? 173 ALA   A CB   1 
ATOM   1324 N  N    . LEU   A 1 174 ? -16.923 -38.422 26.732  1.00 43.00  ? 174 LEU   A N    1 
ATOM   1325 C  CA   . LEU   A 1 174 ? -18.347 -38.036 26.526  1.00 46.31  ? 174 LEU   A CA   1 
ATOM   1326 C  C    . LEU   A 1 174 ? -18.930 -37.525 27.850  1.00 45.94  ? 174 LEU   A C    1 
ATOM   1327 O  O    . LEU   A 1 174 ? -18.582 -38.072 28.933  1.00 44.90  ? 174 LEU   A O    1 
ATOM   1328 C  CB   . LEU   A 1 174 ? -19.170 -39.222 26.015  1.00 45.06  ? 174 LEU   A CB   1 
ATOM   1329 C  CG   . LEU   A 1 174 ? -18.733 -39.817 24.679  1.00 46.67  ? 174 LEU   A CG   1 
ATOM   1330 C  CD1  . LEU   A 1 174 ? -17.684 -40.888 24.886  1.00 53.30  ? 174 LEU   A CD1  1 
ATOM   1331 C  CD2  . LEU   A 1 174 ? -19.917 -40.421 23.956  1.00 45.71  ? 174 LEU   A CD2  1 
ATOM   1332 N  N    . PHE   A 1 175 ? -19.756 -36.485 27.794  1.00 42.45  ? 175 PHE   A N    1 
ATOM   1333 C  CA   . PHE   A 1 175 ? -20.432 -36.006 29.014  1.00 43.90  ? 175 PHE   A CA   1 
ATOM   1334 C  C    . PHE   A 1 175 ? -21.404 -37.114 29.400  1.00 44.05  ? 175 PHE   A C    1 
ATOM   1335 O  O    . PHE   A 1 175 ? -22.038 -37.736 28.506  1.00 48.81  ? 175 PHE   A O    1 
ATOM   1336 C  CB   . PHE   A 1 175 ? -21.074 -34.631 28.845  1.00 44.51  ? 175 PHE   A CB   1 
ATOM   1337 C  CG   . PHE   A 1 175 ? -21.624 -34.089 30.140  1.00 45.02  ? 175 PHE   A CG   1 
ATOM   1338 C  CD1  . PHE   A 1 175 ? -20.763 -33.689 31.151  1.00 47.99  ? 175 PHE   A CD1  1 
ATOM   1339 C  CD2  . PHE   A 1 175 ? -22.987 -34.000 30.358  1.00 41.33  ? 175 PHE   A CD2  1 
ATOM   1340 C  CE1  . PHE   A 1 175 ? -21.240 -33.180 32.350  1.00 46.72  ? 175 PHE   A CE1  1 
ATOM   1341 C  CE2  . PHE   A 1 175 ? -23.457 -33.486 31.553  1.00 48.04  ? 175 PHE   A CE2  1 
ATOM   1342 C  CZ   . PHE   A 1 175 ? -22.590 -33.089 32.549  1.00 46.33  ? 175 PHE   A CZ   1 
ATOM   1343 N  N    . TYR   A 1 176 ? -21.433 -37.420 30.685  1.00 43.10  ? 176 TYR   A N    1 
ATOM   1344 C  CA   . TYR   A 1 176 ? -22.208 -38.549 31.237  1.00 48.90  ? 176 TYR   A CA   1 
ATOM   1345 C  C    . TYR   A 1 176 ? -23.673 -38.405 30.819  1.00 46.63  ? 176 TYR   A C    1 
ATOM   1346 O  O    . TYR   A 1 176 ? -24.360 -39.397 30.570  1.00 47.07  ? 176 TYR   A O    1 
ATOM   1347 C  CB   . TYR   A 1 176 ? -22.045 -38.615 32.757  1.00 54.60  ? 176 TYR   A CB   1 
ATOM   1348 C  CG   . TYR   A 1 176 ? -22.384 -39.978 33.291  1.00 64.78  ? 176 TYR   A CG   1 
ATOM   1349 C  CD1  . TYR   A 1 176 ? -21.545 -41.058 33.074  1.00 65.61  ? 176 TYR   A CD1  1 
ATOM   1350 C  CD2  . TYR   A 1 176 ? -23.576 -40.201 33.954  1.00 69.62  ? 176 TYR   A CD2  1 
ATOM   1351 C  CE1  . TYR   A 1 176 ? -21.874 -42.321 33.528  1.00 72.50  ? 176 TYR   A CE1  1 
ATOM   1352 C  CE2  . TYR   A 1 176 ? -23.915 -41.459 34.420  1.00 67.50  ? 176 TYR   A CE2  1 
ATOM   1353 C  CZ   . TYR   A 1 176 ? -23.063 -42.520 34.206  1.00 68.16  ? 176 TYR   A CZ   1 
ATOM   1354 O  OH   . TYR   A 1 176 ? -23.425 -43.749 34.664  1.00 73.57  ? 176 TYR   A OH   1 
ATOM   1355 N  N    . ALA   A 1 177 ? -24.168 -37.180 30.737  1.00 52.17  ? 177 ALA   A N    1 
ATOM   1356 C  CA   . ALA   A 1 177 ? -25.622 -36.937 30.630  1.00 51.47  ? 177 ALA   A CA   1 
ATOM   1357 C  C    . ALA   A 1 177 ? -26.026 -36.850 29.166  1.00 40.21  ? 177 ALA   A C    1 
ATOM   1358 O  O    . ALA   A 1 177 ? -25.457 -36.082 28.410  1.00 46.15  ? 177 ALA   A O    1 
ATOM   1359 C  CB   . ALA   A 1 177 ? -26.018 -35.703 31.405  1.00 50.18  ? 177 ALA   A CB   1 
ATOM   1360 N  N    . PRO   A 1 178 ? -27.066 -37.594 28.755  1.00 43.94  ? 178 PRO   A N    1 
ATOM   1361 C  CA   . PRO   A 1 178 ? -27.738 -37.334 27.483  1.00 47.87  ? 178 PRO   A CA   1 
ATOM   1362 C  C    . PRO   A 1 178 ? -28.273 -35.895 27.446  1.00 49.01  ? 178 PRO   A C    1 
ATOM   1363 O  O    . PRO   A 1 178 ? -28.708 -35.414 28.469  1.00 47.17  ? 178 PRO   A O    1 
ATOM   1364 C  CB   . PRO   A 1 178 ? -28.919 -38.316 27.438  1.00 44.77  ? 178 PRO   A CB   1 
ATOM   1365 C  CG   . PRO   A 1 178 ? -28.598 -39.361 28.498  1.00 46.29  ? 178 PRO   A CG   1 
ATOM   1366 C  CD   . PRO   A 1 178 ? -27.721 -38.666 29.525  1.00 46.43  ? 178 PRO   A CD   1 
ATOM   1367 N  N    . VAL   A 1 179 ? -28.198 -35.254 26.285  1.00 44.24  ? 179 VAL   A N    1 
ATOM   1368 C  CA   . VAL   A 1 179 ? -28.604 -33.840 26.056  1.00 42.73  ? 179 VAL   A CA   1 
ATOM   1369 C  C    . VAL   A 1 179 ? -29.820 -33.864 25.138  1.00 44.52  ? 179 VAL   A C    1 
ATOM   1370 O  O    . VAL   A 1 179 ? -29.790 -34.641 24.153  1.00 45.09  ? 179 VAL   A O    1 
ATOM   1371 C  CB   . VAL   A 1 179 ? -27.460 -33.053 25.394  1.00 46.06  ? 179 VAL   A CB   1 
ATOM   1372 C  CG1  . VAL   A 1 179 ? -27.789 -31.565 25.249  1.00 46.00  ? 179 VAL   A CG1  1 
ATOM   1373 C  CG2  . VAL   A 1 179 ? -26.152 -33.275 26.139  1.00 43.33  ? 179 VAL   A CG2  1 
ATOM   1374 N  N    . HIS   A 1 180 ? -30.848 -33.080 25.447  1.00 45.31  ? 180 HIS   A N    1 
ATOM   1375 C  CA   . HIS   A 1 180 ? -32.059 -32.936 24.590  1.00 48.55  ? 180 HIS   A CA   1 
ATOM   1376 C  C    . HIS   A 1 180 ? -31.733 -31.873 23.536  1.00 46.39  ? 180 HIS   A C    1 
ATOM   1377 O  O    . HIS   A 1 180 ? -31.817 -30.694 23.869  1.00 46.16  ? 180 HIS   A O    1 
ATOM   1378 C  CB   . HIS   A 1 180 ? -33.334 -32.635 25.410  1.00 41.70  ? 180 HIS   A CB   1 
ATOM   1379 C  CG   . HIS   A 1 180 ? -34.604 -33.065 24.721  1.00 53.81  ? 180 HIS   A CG   1 
ATOM   1380 N  ND1  . HIS   A 1 180 ? -35.848 -33.007 25.316  1.00 52.50  ? 180 HIS   A ND1  1 
ATOM   1381 C  CD2  . HIS   A 1 180 ? -34.824 -33.581 23.488  1.00 57.80  ? 180 HIS   A CD2  1 
ATOM   1382 C  CE1  . HIS   A 1 180 ? -36.761 -33.455 24.486  1.00 59.20  ? 180 HIS   A CE1  1 
ATOM   1383 N  NE2  . HIS   A 1 180 ? -36.162 -33.803 23.355  1.00 59.55  ? 180 HIS   A NE2  1 
ATOM   1384 N  N    . ILE   A 1 181 ? -31.280 -32.270 22.349  1.00 50.05  ? 181 ILE   A N    1 
ATOM   1385 C  CA   . ILE   A 1 181 ? -30.610 -31.323 21.401  1.00 54.47  ? 181 ILE   A CA   1 
ATOM   1386 C  C    . ILE   A 1 181 ? -31.681 -30.650 20.520  1.00 56.94  ? 181 ILE   A C    1 
ATOM   1387 O  O    . ILE   A 1 181 ? -31.480 -29.536 20.012  1.00 60.03  ? 181 ILE   A O    1 
ATOM   1388 C  CB   . ILE   A 1 181 ? -29.500 -32.042 20.605  1.00 51.56  ? 181 ILE   A CB   1 
ATOM   1389 C  CG1  . ILE   A 1 181 ? -28.442 -31.049 20.141  1.00 61.82  ? 181 ILE   A CG1  1 
ATOM   1390 C  CG2  . ILE   A 1 181 ? -30.037 -32.847 19.431  1.00 51.33  ? 181 ILE   A CG2  1 
ATOM   1391 C  CD1  . ILE   A 1 181 ? -27.575 -30.510 21.266  1.00 67.56  ? 181 ILE   A CD1  1 
ATOM   1392 N  N    . TRP   A 1 182 ? -32.830 -31.280 20.353  1.00 56.68  ? 182 TRP   A N    1 
ATOM   1393 C  CA   . TRP   A 1 182 ? -33.912 -30.653 19.571  1.00 60.99  ? 182 TRP   A CA   1 
ATOM   1394 C  C    . TRP   A 1 182 ? -35.252 -31.221 20.012  1.00 62.23  ? 182 TRP   A C    1 
ATOM   1395 O  O    . TRP   A 1 182 ? -35.296 -32.262 20.695  1.00 65.81  ? 182 TRP   A O    1 
ATOM   1396 C  CB   . TRP   A 1 182 ? -33.668 -30.807 18.064  1.00 70.15  ? 182 TRP   A CB   1 
ATOM   1397 C  CG   . TRP   A 1 182 ? -33.783 -32.196 17.493  1.00 72.77  ? 182 TRP   A CG   1 
ATOM   1398 C  CD1  . TRP   A 1 182 ? -32.743 -33.030 17.200  1.00 69.75  ? 182 TRP   A CD1  1 
ATOM   1399 C  CD2  . TRP   A 1 182 ? -34.976 -32.894 17.059  1.00 75.80  ? 182 TRP   A CD2  1 
ATOM   1400 N  NE1  . TRP   A 1 182 ? -33.200 -34.198 16.648  1.00 72.90  ? 182 TRP   A NE1  1 
ATOM   1401 C  CE2  . TRP   A 1 182 ? -34.563 -34.146 16.545  1.00 69.06  ? 182 TRP   A CE2  1 
ATOM   1402 C  CE3  . TRP   A 1 182 ? -36.351 -32.602 17.061  1.00 82.59  ? 182 TRP   A CE3  1 
ATOM   1403 C  CZ2  . TRP   A 1 182 ? -35.459 -35.093 16.054  1.00 68.52  ? 182 TRP   A CZ2  1 
ATOM   1404 C  CZ3  . TRP   A 1 182 ? -37.240 -33.538 16.568  1.00 79.74  ? 182 TRP   A CZ3  1 
ATOM   1405 C  CH2  . TRP   A 1 182 ? -36.798 -34.768 16.079  1.00 74.85  ? 182 TRP   A CH2  1 
ATOM   1406 N  N    . GLU   A 1 183 ? -36.296 -30.529 19.594  1.00 64.65  ? 183 GLU   A N    1 
ATOM   1407 C  CA   . GLU   A 1 183 ? -37.689 -30.724 20.037  1.00 75.47  ? 183 GLU   A CA   1 
ATOM   1408 C  C    . GLU   A 1 183 ? -38.539 -29.979 19.010  1.00 81.65  ? 183 GLU   A C    1 
ATOM   1409 O  O    . GLU   A 1 183 ? -38.271 -28.765 18.840  1.00 76.89  ? 183 GLU   A O    1 
ATOM   1410 C  CB   . GLU   A 1 183 ? -37.785 -30.159 21.452  1.00 76.04  ? 183 GLU   A CB   1 
ATOM   1411 C  CG   . GLU   A 1 183 ? -39.034 -30.511 22.229  1.00 78.74  ? 183 GLU   A CG   1 
ATOM   1412 C  CD   . GLU   A 1 183 ? -38.882 -30.076 23.678  1.00 83.34  ? 183 GLU   A CD   1 
ATOM   1413 O  OE1  . GLU   A 1 183 ? -38.794 -28.843 23.947  1.00 72.70  ? 183 GLU   A OE1  1 
ATOM   1414 O  OE2  . GLU   A 1 183 ? -38.767 -30.974 24.529  1.00 96.30  ? 183 GLU   A OE2  1 
ATOM   1415 N  N    . SER   A 1 184 ? -39.430 -30.678 18.293  1.00 85.51  ? 184 SER   A N    1 
ATOM   1416 C  CA   . SER   A 1 184 ? -40.284 -30.084 17.226  1.00 92.48  ? 184 SER   A CA   1 
ATOM   1417 C  C    . SER   A 1 184 ? -41.163 -28.976 17.840  1.00 93.70  ? 184 SER   A C    1 
ATOM   1418 O  O    . SER   A 1 184 ? -41.430 -27.986 17.139  1.00 94.95  ? 184 SER   A O    1 
ATOM   1419 C  CB   . SER   A 1 184 ? -41.093 -31.138 16.496  1.00 86.90  ? 184 SER   A CB   1 
ATOM   1420 O  OG   . SER   A 1 184 ? -41.862 -31.903 17.416  1.00 87.51  ? 184 SER   A OG   1 
ATOM   1421 N  N    . SER   A 1 185 ? -41.514 -29.095 19.128  1.00 90.27  ? 185 SER   A N    1 
ATOM   1422 C  CA   . SER   A 1 185 ? -42.386 -28.155 19.887  1.00 85.71  ? 185 SER   A CA   1 
ATOM   1423 C  C    . SER   A 1 185 ? -41.626 -26.903 20.350  1.00 81.11  ? 185 SER   A C    1 
ATOM   1424 O  O    . SER   A 1 185 ? -42.164 -26.207 21.218  1.00 78.74  ? 185 SER   A O    1 
ATOM   1425 C  CB   . SER   A 1 185 ? -42.971 -28.845 21.093  1.00 84.83  ? 185 SER   A CB   1 
ATOM   1426 O  OG   . SER   A 1 185 ? -42.076 -28.729 22.196  1.00 80.39  ? 185 SER   A OG   1 
ATOM   1427 N  N    . ALA   A 1 186 ? -40.420 -26.643 19.841  1.00 84.18  ? 186 ALA   A N    1 
ATOM   1428 C  CA   . ALA   A 1 186 ? -39.539 -25.536 20.289  1.00 83.64  ? 186 ALA   A CA   1 
ATOM   1429 C  C    . ALA   A 1 186 ? -39.451 -24.423 19.229  1.00 75.17  ? 186 ALA   A C    1 
ATOM   1430 O  O    . ALA   A 1 186 ? -39.687 -24.685 18.036  1.00 82.06  ? 186 ALA   A O    1 
ATOM   1431 C  CB   . ALA   A 1 186 ? -38.176 -26.087 20.624  1.00 82.06  ? 186 ALA   A CB   1 
ATOM   1432 N  N    . VAL   A 1 187 ? -39.112 -23.215 19.681  1.00 66.73  ? 187 VAL   A N    1 
ATOM   1433 C  CA   . VAL   A 1 187 ? -38.991 -21.964 18.879  1.00 65.21  ? 187 VAL   A CA   1 
ATOM   1434 C  C    . VAL   A 1 187 ? -37.511 -21.723 18.519  1.00 63.93  ? 187 VAL   A C    1 
ATOM   1435 O  O    . VAL   A 1 187 ? -37.227 -21.229 17.419  1.00 64.23  ? 187 VAL   A O    1 
ATOM   1436 C  CB   . VAL   A 1 187 ? -39.600 -20.797 19.684  1.00 66.26  ? 187 VAL   A CB   1 
ATOM   1437 C  CG1  . VAL   A 1 187 ? -39.185 -19.440 19.164  1.00 72.75  ? 187 VAL   A CG1  1 
ATOM   1438 C  CG2  . VAL   A 1 187 ? -41.111 -20.894 19.734  1.00 77.07  ? 187 VAL   A CG2  1 
ATOM   1439 N  N    . VAL   A 1 188 ? -36.595 -22.011 19.437  1.00 57.73  ? 188 VAL   A N    1 
ATOM   1440 C  CA   . VAL   A 1 188 ? -35.130 -21.865 19.218  1.00 66.52  ? 188 VAL   A CA   1 
ATOM   1441 C  C    . VAL   A 1 188 ? -34.457 -22.969 20.049  1.00 62.50  ? 188 VAL   A C    1 
ATOM   1442 O  O    . VAL   A 1 188 ? -34.704 -23.088 21.260  1.00 54.56  ? 188 VAL   A O    1 
ATOM   1443 C  CB   . VAL   A 1 188 ? -34.622 -20.427 19.497  1.00 66.71  ? 188 VAL   A CB   1 
ATOM   1444 C  CG1  . VAL   A 1 188 ? -35.277 -19.828 20.725  1.00 71.61  ? 188 VAL   A CG1  1 
ATOM   1445 C  CG2  . VAL   A 1 188 ? -33.093 -20.308 19.590  1.00 59.56  ? 188 VAL   A CG2  1 
ATOM   1446 N  N    . ALA   A 1 189 ? -33.812 -23.881 19.341  1.00 59.29  ? 189 ALA   A N    1 
ATOM   1447 C  CA   . ALA   A 1 189 ? -32.878 -24.878 19.885  1.00 60.74  ? 189 ALA   A CA   1 
ATOM   1448 C  C    . ALA   A 1 189 ? -31.512 -24.270 19.573  1.00 58.17  ? 189 ALA   A C    1 
ATOM   1449 O  O    . ALA   A 1 189 ? -31.420 -23.583 18.561  1.00 64.37  ? 189 ALA   A O    1 
ATOM   1450 C  CB   . ALA   A 1 189 ? -33.134 -26.247 19.269  1.00 56.52  ? 189 ALA   A CB   1 
ATOM   1451 N  N    . SER   A 1 190 ? -30.556 -24.340 20.490  1.00 53.79  ? 190 SER   A N    1 
ATOM   1452 C  CA   . SER   A 1 190 ? -29.198 -23.802 20.275  1.00 47.33  ? 190 SER   A CA   1 
ATOM   1453 C  C    . SER   A 1 190 ? -28.237 -24.550 21.193  1.00 45.99  ? 190 SER   A C    1 
ATOM   1454 O  O    . SER   A 1 190 ? -28.653 -24.926 22.323  1.00 45.34  ? 190 SER   A O    1 
ATOM   1455 C  CB   . SER   A 1 190 ? -29.178 -22.332 20.513  1.00 46.87  ? 190 SER   A CB   1 
ATOM   1456 O  OG   . SER   A 1 190 ? -29.142 -22.052 21.896  1.00 52.92  ? 190 SER   A OG   1 
ATOM   1457 N  N    . PHE   A 1 191 ? -27.002 -24.733 20.749  1.00 38.56  ? 191 PHE   A N    1 
ATOM   1458 C  CA   . PHE   A 1 191 ? -25.903 -25.155 21.648  1.00 43.99  ? 191 PHE   A CA   1 
ATOM   1459 C  C    . PHE   A 1 191 ? -24.616 -24.399 21.317  1.00 42.09  ? 191 PHE   A C    1 
ATOM   1460 O  O    . PHE   A 1 191 ? -24.559 -23.761 20.267  1.00 41.35  ? 191 PHE   A O    1 
ATOM   1461 C  CB   . PHE   A 1 191 ? -25.718 -26.669 21.564  1.00 41.90  ? 191 PHE   A CB   1 
ATOM   1462 C  CG   . PHE   A 1 191 ? -25.294 -27.179 20.221  1.00 40.59  ? 191 PHE   A CG   1 
ATOM   1463 C  CD1  . PHE   A 1 191 ? -23.955 -27.222 19.873  1.00 44.96  ? 191 PHE   A CD1  1 
ATOM   1464 C  CD2  . PHE   A 1 191 ? -26.216 -27.722 19.348  1.00 43.73  ? 191 PHE   A CD2  1 
ATOM   1465 C  CE1  . PHE   A 1 191 ? -23.558 -27.739 18.647  1.00 45.65  ? 191 PHE   A CE1  1 
ATOM   1466 C  CE2  . PHE   A 1 191 ? -25.815 -28.229 18.116  1.00 45.10  ? 191 PHE   A CE2  1 
ATOM   1467 C  CZ   . PHE   A 1 191 ? -24.489 -28.238 17.764  1.00 41.59  ? 191 PHE   A CZ   1 
ATOM   1468 N  N    . GLU   A 1 192 ? -23.639 -24.467 22.218  1.00 36.79  ? 192 GLU   A N    1 
ATOM   1469 C  CA   . GLU   A 1 192 ? -22.255 -24.016 21.978  1.00 41.63  ? 192 GLU   A CA   1 
ATOM   1470 C  C    . GLU   A 1 192 ? -21.316 -24.967 22.724  1.00 43.26  ? 192 GLU   A C    1 
ATOM   1471 O  O    . GLU   A 1 192 ? -21.739 -25.581 23.699  1.00 50.20  ? 192 GLU   A O    1 
ATOM   1472 C  CB   . GLU   A 1 192 ? -22.056 -22.566 22.409  1.00 49.69  ? 192 GLU   A CB   1 
ATOM   1473 C  CG   . GLU   A 1 192 ? -22.888 -22.176 23.603  1.00 67.39  ? 192 GLU   A CG   1 
ATOM   1474 C  CD   . GLU   A 1 192 ? -22.535 -20.849 24.257  1.00 83.04  ? 192 GLU   A CD   1 
ATOM   1475 O  OE1  . GLU   A 1 192 ? -21.401 -20.367 24.054  1.00 84.72  ? 192 GLU   A OE1  1 
ATOM   1476 O  OE2  . GLU   A 1 192 ? -23.392 -20.315 24.997  1.00 86.92  ? 192 GLU   A OE2  1 
ATOM   1477 N  N    . ALA   A 1 193 ? -20.107 -25.136 22.229  1.00 36.58  ? 193 ALA   A N    1 
ATOM   1478 C  CA   . ALA   A 1 193 ? -19.032 -25.825 22.941  1.00 43.74  ? 193 ALA   A CA   1 
ATOM   1479 C  C    . ALA   A 1 193 ? -17.773 -24.994 22.788  1.00 39.98  ? 193 ALA   A C    1 
ATOM   1480 O  O    . ALA   A 1 193 ? -17.649 -24.283 21.792  1.00 37.51  ? 193 ALA   A O    1 
ATOM   1481 C  CB   . ALA   A 1 193 ? -18.846 -27.220 22.397  1.00 49.24  ? 193 ALA   A CB   1 
ATOM   1482 N  N    . THR   A 1 194 ? -16.886 -25.118 23.762  1.00 42.84  ? 194 THR   A N    1 
ATOM   1483 C  CA   . THR   A 1 194 ? -15.565 -24.451 23.788  1.00 43.94  ? 194 THR   A CA   1 
ATOM   1484 C  C    . THR   A 1 194 ? -14.583 -25.417 24.417  1.00 38.97  ? 194 THR   A C    1 
ATOM   1485 O  O    . THR   A 1 194 ? -14.905 -26.015 25.412  1.00 45.69  ? 194 THR   A O    1 
ATOM   1486 C  CB   . THR   A 1 194 ? -15.619 -23.135 24.566  1.00 45.10  ? 194 THR   A CB   1 
ATOM   1487 O  OG1  . THR   A 1 194 ? -16.527 -22.279 23.870  1.00 59.98  ? 194 THR   A OG1  1 
ATOM   1488 C  CG2  . THR   A 1 194 ? -14.281 -22.452 24.663  1.00 43.37  ? 194 THR   A CG2  1 
ATOM   1489 N  N    . PHE   A 1 195 ? -13.425 -25.579 23.836  1.00 40.04  ? 195 PHE   A N    1 
ATOM   1490 C  CA   . PHE   A 1 195 ? -12.351 -26.346 24.493  1.00 42.71  ? 195 PHE   A CA   1 
ATOM   1491 C  C    . PHE   A 1 195 ? -11.058 -25.674 24.104  1.00 41.70  ? 195 PHE   A C    1 
ATOM   1492 O  O    . PHE   A 1 195 ? -11.023 -24.978 23.079  1.00 40.02  ? 195 PHE   A O    1 
ATOM   1493 C  CB   . PHE   A 1 195 ? -12.381 -27.831 24.104  1.00 46.36  ? 195 PHE   A CB   1 
ATOM   1494 C  CG   . PHE   A 1 195 ? -12.204 -28.170 22.638  1.00 43.22  ? 195 PHE   A CG   1 
ATOM   1495 C  CD1  . PHE   A 1 195 ? -13.283 -28.193 21.769  1.00 43.45  ? 195 PHE   A CD1  1 
ATOM   1496 C  CD2  . PHE   A 1 195 ? -10.964 -28.519 22.135  1.00 40.57  ? 195 PHE   A CD2  1 
ATOM   1497 C  CE1  . PHE   A 1 195 ? -13.110 -28.521 20.433  1.00 47.02  ? 195 PHE   A CE1  1 
ATOM   1498 C  CE2  . PHE   A 1 195 ? -10.801 -28.869 20.808  1.00 39.46  ? 195 PHE   A CE2  1 
ATOM   1499 C  CZ   . PHE   A 1 195 ? -11.869 -28.859 19.957  1.00 44.59  ? 195 PHE   A CZ   1 
ATOM   1500 N  N    . THR   A 1 196 ? -10.058 -25.902 24.931  1.00 40.78  ? 196 THR   A N    1 
ATOM   1501 C  CA   . THR   A 1 196 ? -8.663  -25.471 24.718  1.00 39.82  ? 196 THR   A CA   1 
ATOM   1502 C  C    . THR   A 1 196 ? -7.853  -26.761 24.640  1.00 41.66  ? 196 THR   A C    1 
ATOM   1503 O  O    . THR   A 1 196 ? -8.214  -27.736 25.354  1.00 38.81  ? 196 THR   A O    1 
ATOM   1504 C  CB   . THR   A 1 196 ? -8.194  -24.505 25.813  1.00 36.88  ? 196 THR   A CB   1 
ATOM   1505 O  OG1  . THR   A 1 196 ? -8.227  -25.241 27.025  1.00 40.62  ? 196 THR   A OG1  1 
ATOM   1506 C  CG2  . THR   A 1 196 ? -9.092  -23.306 25.987  1.00 39.35  ? 196 THR   A CG2  1 
ATOM   1507 N  N    . PHE   A 1 197 ? -6.839  -26.778 23.769  1.00 42.96  ? 197 PHE   A N    1 
ATOM   1508 C  CA   . PHE   A 1 197 ? -6.093  -27.999 23.395  1.00 40.67  ? 197 PHE   A CA   1 
ATOM   1509 C  C    . PHE   A 1 197 ? -4.637  -27.616 23.166  1.00 45.74  ? 197 PHE   A C    1 
ATOM   1510 O  O    . PHE   A 1 197 ? -4.335  -26.423 22.893  1.00 38.56  ? 197 PHE   A O    1 
ATOM   1511 C  CB   . PHE   A 1 197 ? -6.726  -28.620 22.152  1.00 40.32  ? 197 PHE   A CB   1 
ATOM   1512 C  CG   . PHE   A 1 197 ? -6.741  -27.672 20.974  1.00 42.54  ? 197 PHE   A CG   1 
ATOM   1513 C  CD1  . PHE   A 1 197 ? -5.650  -27.589 20.125  1.00 41.04  ? 197 PHE   A CD1  1 
ATOM   1514 C  CD2  . PHE   A 1 197 ? -7.814  -26.830 20.748  1.00 38.78  ? 197 PHE   A CD2  1 
ATOM   1515 C  CE1  . PHE   A 1 197 ? -5.645  -26.695 19.066  1.00 40.94  ? 197 PHE   A CE1  1 
ATOM   1516 C  CE2  . PHE   A 1 197 ? -7.805  -25.941 19.687  1.00 42.78  ? 197 PHE   A CE2  1 
ATOM   1517 C  CZ   . PHE   A 1 197 ? -6.718  -25.872 18.847  1.00 39.24  ? 197 PHE   A CZ   1 
ATOM   1518 N  N    . LEU   A 1 198 ? -3.780  -28.615 23.358  1.00 45.45  ? 198 LEU   A N    1 
ATOM   1519 C  CA   . LEU   A 1 198 ? -2.331  -28.547 23.135  1.00 44.42  ? 198 LEU   A CA   1 
ATOM   1520 C  C    . LEU   A 1 198 ? -1.978  -29.788 22.306  1.00 49.91  ? 198 LEU   A C    1 
ATOM   1521 O  O    . LEU   A 1 198 ? -2.119  -30.921 22.810  1.00 52.63  ? 198 LEU   A O    1 
ATOM   1522 C  CB   . LEU   A 1 198 ? -1.640  -28.501 24.497  1.00 48.78  ? 198 LEU   A CB   1 
ATOM   1523 C  CG   . LEU   A 1 198 ? -0.173  -28.060 24.525  1.00 55.05  ? 198 LEU   A CG   1 
ATOM   1524 C  CD1  . LEU   A 1 198 ? 0.378   -28.170 25.944  1.00 57.76  ? 198 LEU   A CD1  1 
ATOM   1525 C  CD2  . LEU   A 1 198 ? 0.680   -28.901 23.586  1.00 59.51  ? 198 LEU   A CD2  1 
ATOM   1526 N  N    . ILE   A 1 199 ? -1.618  -29.561 21.047  1.00 45.98  ? 199 ILE   A N    1 
ATOM   1527 C  CA   . ILE   A 1 199 ? -1.163  -30.608 20.104  1.00 47.70  ? 199 ILE   A CA   1 
ATOM   1528 C  C    . ILE   A 1 199 ? 0.310   -30.357 19.865  1.00 49.42  ? 199 ILE   A C    1 
ATOM   1529 O  O    . ILE   A 1 199 ? 0.637   -29.273 19.380  1.00 57.27  ? 199 ILE   A O    1 
ATOM   1530 C  CB   . ILE   A 1 199 ? -1.947  -30.554 18.795  1.00 43.93  ? 199 ILE   A CB   1 
ATOM   1531 C  CG1  . ILE   A 1 199 ? -3.438  -30.741 19.060  1.00 43.22  ? 199 ILE   A CG1  1 
ATOM   1532 C  CG2  . ILE   A 1 199 ? -1.390  -31.566 17.809  1.00 46.02  ? 199 ILE   A CG2  1 
ATOM   1533 C  CD1  . ILE   A 1 199 ? -4.284  -30.323 17.892  1.00 44.14  ? 199 ILE   A CD1  1 
ATOM   1534 N  N    . LYS   A 1 200 ? 1.129   -31.319 20.268  1.00 55.46  ? 200 LYS   A N    1 
ATOM   1535 C  CA   . LYS   A 1 200 ? 2.606   -31.253 20.294  1.00 58.46  ? 200 LYS   A CA   1 
ATOM   1536 C  C    . LYS   A 1 200 ? 3.086   -32.523 19.586  1.00 58.00  ? 200 LYS   A C    1 
ATOM   1537 O  O    . LYS   A 1 200 ? 2.635   -33.648 19.896  1.00 46.82  ? 200 LYS   A O    1 
ATOM   1538 C  CB   . LYS   A 1 200 ? 3.138   -31.074 21.727  1.00 66.17  ? 200 LYS   A CB   1 
ATOM   1539 C  CG   . LYS   A 1 200 ? 4.640   -31.279 21.921  1.00 82.33  ? 200 LYS   A CG   1 
ATOM   1540 C  CD   . LYS   A 1 200 ? 5.443   -30.008 22.187  1.00 101.49 ? 200 LYS   A CD   1 
ATOM   1541 C  CE   . LYS   A 1 200 ? 6.668   -29.873 21.293  1.00 114.39 ? 200 LYS   A CE   1 
ATOM   1542 N  NZ   . LYS   A 1 200 ? 7.354   -28.566 21.465  1.00 111.26 ? 200 LYS   A NZ   1 
ATOM   1543 N  N    . SER   A 1 201 ? 3.951   -32.335 18.614  1.00 56.66  ? 201 SER   A N    1 
ATOM   1544 C  CA   . SER   A 1 201 ? 4.584   -33.440 17.883  1.00 60.87  ? 201 SER   A CA   1 
ATOM   1545 C  C    . SER   A 1 201 ? 6.096   -33.284 17.972  1.00 57.35  ? 201 SER   A C    1 
ATOM   1546 O  O    . SER   A 1 201 ? 6.578   -32.188 17.736  1.00 59.50  ? 201 SER   A O    1 
ATOM   1547 C  CB   . SER   A 1 201 ? 4.085   -33.434 16.478  1.00 55.35  ? 201 SER   A CB   1 
ATOM   1548 O  OG   . SER   A 1 201 ? 4.081   -34.760 15.988  1.00 60.63  ? 201 SER   A OG   1 
ATOM   1549 N  N    . PRO   A 1 202 ? 6.871   -34.360 18.240  1.00 65.29  ? 202 PRO   A N    1 
ATOM   1550 C  CA   . PRO   A 1 202 ? 8.312   -34.351 17.982  1.00 79.03  ? 202 PRO   A CA   1 
ATOM   1551 C  C    . PRO   A 1 202 ? 8.563   -34.356 16.464  1.00 82.68  ? 202 PRO   A C    1 
ATOM   1552 O  O    . PRO   A 1 202 ? 9.518   -33.753 16.046  1.00 98.64  ? 202 PRO   A O    1 
ATOM   1553 C  CB   . PRO   A 1 202 ? 8.809   -35.648 18.618  1.00 81.85  ? 202 PRO   A CB   1 
ATOM   1554 C  CG   . PRO   A 1 202 ? 7.610   -36.579 18.507  1.00 84.87  ? 202 PRO   A CG   1 
ATOM   1555 C  CD   . PRO   A 1 202 ? 6.383   -35.692 18.621  1.00 76.13  ? 202 PRO   A CD   1 
ATOM   1556 N  N    . ASP   A 1 203 ? 7.662   -34.980 15.690  1.00 92.21  ? 203 ASP   A N    1 
ATOM   1557 C  CA   . ASP   A 1 203 ? 7.669   -35.047 14.198  1.00 102.44 ? 203 ASP   A CA   1 
ATOM   1558 C  C    . ASP   A 1 203 ? 7.593   -33.626 13.591  1.00 101.06 ? 203 ASP   A C    1 
ATOM   1559 O  O    . ASP   A 1 203 ? 7.167   -32.675 14.265  1.00 86.75  ? 203 ASP   A O    1 
ATOM   1560 C  CB   . ASP   A 1 203 ? 6.526   -35.927 13.633  1.00 99.39  ? 203 ASP   A CB   1 
ATOM   1561 C  CG   . ASP   A 1 203 ? 6.474   -37.425 14.000  1.00 117.14 ? 203 ASP   A CG   1 
ATOM   1562 O  OD1  . ASP   A 1 203 ? 7.559   -38.026 14.253  1.00 111.72 ? 203 ASP   A OD1  1 
ATOM   1563 O  OD2  . ASP   A 1 203 ? 5.327   -38.018 14.001  1.00 85.44  ? 203 ASP   A OD2  1 
ATOM   1564 N  N    . SER   A 1 204 ? 8.041   -33.498 12.341  1.00 111.30 ? 204 SER   A N    1 
ATOM   1565 C  CA   . SER   A 1 204 ? 7.756   -32.376 11.408  1.00 107.96 ? 204 SER   A CA   1 
ATOM   1566 C  C    . SER   A 1 204 ? 6.325   -32.528 10.853  1.00 108.74 ? 204 SER   A C    1 
ATOM   1567 O  O    . SER   A 1 204 ? 5.763   -31.522 10.358  1.00 86.92  ? 204 SER   A O    1 
ATOM   1568 C  CB   . SER   A 1 204 ? 8.797   -32.329 10.291  1.00 103.51 ? 204 SER   A CB   1 
ATOM   1569 O  OG   . SER   A 1 204 ? 8.663   -33.444 9.406   1.00 81.24  ? 204 SER   A OG   1 
ATOM   1570 N  N    . HIS   A 1 205 ? 5.761   -33.745 10.899  1.00 101.28 ? 205 HIS   A N    1 
ATOM   1571 C  CA   . HIS   A 1 205 ? 4.381   -34.077 10.434  1.00 99.09  ? 205 HIS   A CA   1 
ATOM   1572 C  C    . HIS   A 1 205 ? 3.639   -34.720 11.608  1.00 83.64  ? 205 HIS   A C    1 
ATOM   1573 O  O    . HIS   A 1 205 ? 3.913   -35.863 11.981  1.00 74.10  ? 205 HIS   A O    1 
ATOM   1574 C  CB   . HIS   A 1 205 ? 4.412   -34.914 9.134   1.00 99.38  ? 205 HIS   A CB   1 
ATOM   1575 C  CG   . HIS   A 1 205 ? 5.652   -35.734 8.994   1.00 106.23 ? 205 HIS   A CG   1 
ATOM   1576 N  ND1  . HIS   A 1 205 ? 6.636   -35.452 8.051   1.00 113.92 ? 205 HIS   A ND1  1 
ATOM   1577 C  CD2  . HIS   A 1 205 ? 6.112   -36.777 9.723   1.00 109.29 ? 205 HIS   A CD2  1 
ATOM   1578 C  CE1  . HIS   A 1 205 ? 7.634   -36.310 8.187   1.00 111.04 ? 205 HIS   A CE1  1 
ATOM   1579 N  NE2  . HIS   A 1 205 ? 7.331   -37.139 9.201   1.00 118.43 ? 205 HIS   A NE2  1 
ATOM   1580 N  N    . PRO   A 1 206 ? 2.769   -33.959 12.313  1.00 64.99  ? 206 PRO   A N    1 
ATOM   1581 C  CA   . PRO   A 1 206 ? 1.853   -34.547 13.297  1.00 58.14  ? 206 PRO   A CA   1 
ATOM   1582 C  C    . PRO   A 1 206 ? 0.569   -35.162 12.689  1.00 50.26  ? 206 PRO   A C    1 
ATOM   1583 O  O    . PRO   A 1 206 ? 0.153   -34.755 11.584  1.00 47.70  ? 206 PRO   A O    1 
ATOM   1584 C  CB   . PRO   A 1 206 ? 1.523   -33.309 14.139  1.00 52.18  ? 206 PRO   A CB   1 
ATOM   1585 C  CG   . PRO   A 1 206 ? 1.439   -32.227 13.110  1.00 53.11  ? 206 PRO   A CG   1 
ATOM   1586 C  CD   . PRO   A 1 206 ? 2.642   -32.494 12.235  1.00 51.22  ? 206 PRO   A CD   1 
ATOM   1587 N  N    . ALA   A 1 207 ? -0.062  -36.078 13.437  1.00 43.46  ? 207 ALA   A N    1 
ATOM   1588 C  CA   . ALA   A 1 207 ? -1.375  -36.701 13.102  1.00 49.67  ? 207 ALA   A CA   1 
ATOM   1589 C  C    . ALA   A 1 207 ? -2.047  -37.210 14.379  1.00 44.24  ? 207 ALA   A C    1 
ATOM   1590 O  O    . ALA   A 1 207 ? -1.362  -37.483 15.369  1.00 44.51  ? 207 ALA   A O    1 
ATOM   1591 C  CB   . ALA   A 1 207 ? -1.184  -37.828 12.088  1.00 46.62  ? 207 ALA   A CB   1 
ATOM   1592 N  N    . ASP   A 1 208 ? -3.372  -37.407 14.348  1.00 42.81  ? 208 ASP   A N    1 
ATOM   1593 C  CA   . ASP   A 1 208 ? -4.239  -37.246 13.185  1.00 40.89  ? 208 ASP   A CA   1 
ATOM   1594 C  C    . ASP   A 1 208 ? -5.250  -36.095 13.386  1.00 41.60  ? 208 ASP   A C    1 
ATOM   1595 O  O    . ASP   A 1 208 ? -5.688  -35.517 12.369  1.00 41.76  ? 208 ASP   A O    1 
ATOM   1596 C  CB   . ASP   A 1 208 ? -4.908  -38.584 12.887  1.00 42.90  ? 208 ASP   A CB   1 
ATOM   1597 C  CG   . ASP   A 1 208 ? -4.173  -39.365 11.816  1.00 46.49  ? 208 ASP   A CG   1 
ATOM   1598 O  OD1  . ASP   A 1 208 ? -4.445  -39.083 10.647  1.00 44.17  ? 208 ASP   A OD1  1 
ATOM   1599 O  OD2  . ASP   A 1 208 ? -3.313  -40.223 12.167  1.00 45.79  ? 208 ASP   A OD2  1 
ATOM   1600 N  N    . GLY   A 1 209 ? -5.569  -35.747 14.643  1.00 40.42  ? 209 GLY   A N    1 
ATOM   1601 C  CA   . GLY   A 1 209 ? -6.322  -34.542 15.030  1.00 41.27  ? 209 GLY   A CA   1 
ATOM   1602 C  C    . GLY   A 1 209 ? -7.279  -34.749 16.207  1.00 40.11  ? 209 GLY   A C    1 
ATOM   1603 O  O    . GLY   A 1 209 ? -7.190  -35.745 16.940  1.00 42.92  ? 209 GLY   A O    1 
ATOM   1604 N  N    . ILE   A 1 210 ? -8.166  -33.784 16.384  1.00 40.61  ? 210 ILE   A N    1 
ATOM   1605 C  CA   . ILE   A 1 210 ? -9.166  -33.711 17.477  1.00 40.12  ? 210 ILE   A CA   1 
ATOM   1606 C  C    . ILE   A 1 210 ? -10.475 -33.293 16.836  1.00 43.41  ? 210 ILE   A C    1 
ATOM   1607 O  O    . ILE   A 1 210 ? -10.404 -32.568 15.834  1.00 41.12  ? 210 ILE   A O    1 
ATOM   1608 C  CB   . ILE   A 1 210 ? -8.753  -32.719 18.561  1.00 38.57  ? 210 ILE   A CB   1 
ATOM   1609 C  CG1  . ILE   A 1 210 ? -7.421  -33.129 19.186  1.00 46.34  ? 210 ILE   A CG1  1 
ATOM   1610 C  CG2  . ILE   A 1 210 ? -9.849  -32.616 19.601  1.00 44.53  ? 210 ILE   A CG2  1 
ATOM   1611 C  CD1  . ILE   A 1 210 ? -6.885  -32.105 20.144  1.00 47.81  ? 210 ILE   A CD1  1 
ATOM   1612 N  N    . ALA   A 1 211 ? -11.579 -33.812 17.379  1.00 43.09  ? 211 ALA   A N    1 
ATOM   1613 C  CA   . ALA   A 1 211 ? -12.970 -33.491 17.009  1.00 45.78  ? 211 ALA   A CA   1 
ATOM   1614 C  C    . ALA   A 1 211 ? -13.816 -33.318 18.282  1.00 43.12  ? 211 ALA   A C    1 
ATOM   1615 O  O    . ALA   A 1 211 ? -13.598 -34.067 19.279  1.00 36.48  ? 211 ALA   A O    1 
ATOM   1616 C  CB   . ALA   A 1 211 ? -13.539 -34.575 16.115  1.00 45.76  ? 211 ALA   A CB   1 
ATOM   1617 N  N    . PHE   A 1 212 ? -14.705 -32.320 18.250  1.00 40.65  ? 212 PHE   A N    1 
ATOM   1618 C  CA   . PHE   A 1 212 ? -15.923 -32.243 19.082  1.00 41.32  ? 212 PHE   A CA   1 
ATOM   1619 C  C    . PHE   A 1 212 ? -17.031 -32.943 18.277  1.00 40.06  ? 212 PHE   A C    1 
ATOM   1620 O  O    . PHE   A 1 212 ? -17.106 -32.733 17.057  1.00 42.99  ? 212 PHE   A O    1 
ATOM   1621 C  CB   . PHE   A 1 212 ? -16.218 -30.793 19.474  1.00 40.05  ? 212 PHE   A CB   1 
ATOM   1622 C  CG   . PHE   A 1 212 ? -17.619 -30.620 19.973  1.00 36.43  ? 212 PHE   A CG   1 
ATOM   1623 C  CD1  . PHE   A 1 212 ? -17.907 -30.789 21.310  1.00 38.76  ? 212 PHE   A CD1  1 
ATOM   1624 C  CD2  . PHE   A 1 212 ? -18.658 -30.399 19.086  1.00 37.92  ? 212 PHE   A CD2  1 
ATOM   1625 C  CE1  . PHE   A 1 212 ? -19.204 -30.654 21.773  1.00 40.27  ? 212 PHE   A CE1  1 
ATOM   1626 C  CE2  . PHE   A 1 212 ? -19.957 -30.262 19.543  1.00 40.82  ? 212 PHE   A CE2  1 
ATOM   1627 C  CZ   . PHE   A 1 212 ? -20.228 -30.386 20.888  1.00 41.74  ? 212 PHE   A CZ   1 
ATOM   1628 N  N    . PHE   A 1 213 ? -17.839 -33.797 18.912  1.00 38.33  ? 213 PHE   A N    1 
ATOM   1629 C  CA   . PHE   A 1 213 ? -18.867 -34.589 18.194  1.00 41.53  ? 213 PHE   A CA   1 
ATOM   1630 C  C    . PHE   A 1 213 ? -20.131 -34.762 19.050  1.00 46.60  ? 213 PHE   A C    1 
ATOM   1631 O  O    . PHE   A 1 213 ? -20.127 -34.710 20.297  1.00 43.92  ? 213 PHE   A O    1 
ATOM   1632 C  CB   . PHE   A 1 213 ? -18.301 -35.938 17.749  1.00 43.53  ? 213 PHE   A CB   1 
ATOM   1633 C  CG   . PHE   A 1 213 ? -18.072 -36.935 18.854  1.00 41.12  ? 213 PHE   A CG   1 
ATOM   1634 C  CD1  . PHE   A 1 213 ? -16.944 -36.863 19.657  1.00 40.99  ? 213 PHE   A CD1  1 
ATOM   1635 C  CD2  . PHE   A 1 213 ? -18.997 -37.939 19.104  1.00 45.56  ? 213 PHE   A CD2  1 
ATOM   1636 C  CE1  . PHE   A 1 213 ? -16.728 -37.796 20.663  1.00 41.87  ? 213 PHE   A CE1  1 
ATOM   1637 C  CE2  . PHE   A 1 213 ? -18.788 -38.870 20.116  1.00 47.04  ? 213 PHE   A CE2  1 
ATOM   1638 C  CZ   . PHE   A 1 213 ? -17.654 -38.789 20.900  1.00 43.64  ? 213 PHE   A CZ   1 
ATOM   1639 N  N    . ILE   A 1 214 ? -21.223 -34.939 18.329  1.00 42.40  ? 214 ILE   A N    1 
ATOM   1640 C  CA   . ILE   A 1 214 ? -22.571 -35.204 18.867  1.00 43.90  ? 214 ILE   A CA   1 
ATOM   1641 C  C    . ILE   A 1 214 ? -22.962 -36.540 18.260  1.00 42.48  ? 214 ILE   A C    1 
ATOM   1642 O  O    . ILE   A 1 214 ? -22.706 -36.731 17.060  1.00 42.19  ? 214 ILE   A O    1 
ATOM   1643 C  CB   . ILE   A 1 214 ? -23.531 -34.067 18.493  1.00 43.91  ? 214 ILE   A CB   1 
ATOM   1644 C  CG1  . ILE   A 1 214 ? -22.903 -32.716 18.806  1.00 46.73  ? 214 ILE   A CG1  1 
ATOM   1645 C  CG2  . ILE   A 1 214 ? -24.873 -34.233 19.184  1.00 47.60  ? 214 ILE   A CG2  1 
ATOM   1646 C  CD1  . ILE   A 1 214 ? -23.718 -31.551 18.339  1.00 52.10  ? 214 ILE   A CD1  1 
ATOM   1647 N  N    . SER   A 1 215 ? -23.489 -37.450 19.069  1.00 44.12  ? 215 SER   A N    1 
ATOM   1648 C  CA   . SER   A 1 215 ? -23.764 -38.845 18.646  1.00 46.42  ? 215 SER   A CA   1 
ATOM   1649 C  C    . SER   A 1 215 ? -25.012 -39.352 19.356  1.00 47.13  ? 215 SER   A C    1 
ATOM   1650 O  O    . SER   A 1 215 ? -25.493 -38.665 20.308  1.00 48.21  ? 215 SER   A O    1 
ATOM   1651 C  CB   . SER   A 1 215 ? -22.598 -39.743 18.948  1.00 49.69  ? 215 SER   A CB   1 
ATOM   1652 O  OG   . SER   A 1 215 ? -22.495 -39.950 20.366  1.00 50.06  ? 215 SER   A OG   1 
ATOM   1653 N  N    . ASN   A 1 216 ? -25.466 -40.527 18.919  1.00 48.23  ? 216 ASN   A N    1 
ATOM   1654 C  CA   . ASN   A 1 216 ? -26.422 -41.391 19.656  1.00 51.24  ? 216 ASN   A CA   1 
ATOM   1655 C  C    . ASN   A 1 216 ? -25.817 -41.610 21.048  1.00 49.25  ? 216 ASN   A C    1 
ATOM   1656 O  O    . ASN   A 1 216 ? -24.589 -41.617 21.130  1.00 52.96  ? 216 ASN   A O    1 
ATOM   1657 C  CB   . ASN   A 1 216 ? -26.808 -42.648 18.857  1.00 53.33  ? 216 ASN   A CB   1 
ATOM   1658 C  CG   . ASN   A 1 216 ? -25.652 -43.386 18.218  1.00 60.87  ? 216 ASN   A CG   1 
ATOM   1659 O  OD1  . ASN   A 1 216 ? -25.010 -42.862 17.306  1.00 64.21  ? 216 ASN   A OD1  1 
ATOM   1660 N  ND2  . ASN   A 1 216 ? -25.395 -44.605 18.681  1.00 56.15  ? 216 ASN   A ND2  1 
ATOM   1661 N  N    . ILE   A 1 217 ? -26.661 -41.714 22.085  1.00 47.92  ? 217 ILE   A N    1 
ATOM   1662 C  CA   . ILE   A 1 217 ? -26.259 -41.768 23.516  1.00 50.05  ? 217 ILE   A CA   1 
ATOM   1663 C  C    . ILE   A 1 217 ? -25.300 -42.946 23.733  1.00 45.25  ? 217 ILE   A C    1 
ATOM   1664 O  O    . ILE   A 1 217 ? -24.458 -42.860 24.626  1.00 53.70  ? 217 ILE   A O    1 
ATOM   1665 C  CB   . ILE   A 1 217 ? -27.482 -41.847 24.467  1.00 55.02  ? 217 ILE   A CB   1 
ATOM   1666 C  CG1  . ILE   A 1 217 ? -28.156 -43.219 24.414  1.00 74.64  ? 217 ILE   A CG1  1 
ATOM   1667 C  CG2  . ILE   A 1 217 ? -28.469 -40.713 24.209  1.00 57.04  ? 217 ILE   A CG2  1 
ATOM   1668 C  CD1  . ILE   A 1 217 ? -29.281 -43.420 25.414  1.00 84.72  ? 217 ILE   A CD1  1 
ATOM   1669 N  N    . ASP   A 1 218 ? -25.439 -44.019 22.972  1.00 44.55  ? 218 ASP   A N    1 
ATOM   1670 C  CA   . ASP   A 1 218 ? -24.725 -45.307 23.184  1.00 52.01  ? 218 ASP   A CA   1 
ATOM   1671 C  C    . ASP   A 1 218 ? -23.456 -45.354 22.315  1.00 53.25  ? 218 ASP   A C    1 
ATOM   1672 O  O    . ASP   A 1 218 ? -22.790 -46.412 22.302  1.00 56.82  ? 218 ASP   A O    1 
ATOM   1673 C  CB   . ASP   A 1 218 ? -25.645 -46.495 22.877  1.00 59.54  ? 218 ASP   A CB   1 
ATOM   1674 C  CG   . ASP   A 1 218 ? -26.376 -46.420 21.535  1.00 71.64  ? 218 ASP   A CG   1 
ATOM   1675 O  OD1  . ASP   A 1 218 ? -27.068 -45.389 21.262  1.00 77.21  ? 218 ASP   A OD1  1 
ATOM   1676 O  OD2  . ASP   A 1 218 ? -26.295 -47.403 20.787  1.00 70.35  ? 218 ASP   A OD2  1 
ATOM   1677 N  N    . SER   A 1 219 ? -23.112 -44.259 21.634  1.00 45.95  ? 219 SER   A N    1 
ATOM   1678 C  CA   . SER   A 1 219 ? -21.933 -44.190 20.737  1.00 55.23  ? 219 SER   A CA   1 
ATOM   1679 C  C    . SER   A 1 219 ? -20.710 -44.803 21.419  1.00 51.06  ? 219 SER   A C    1 
ATOM   1680 O  O    . SER   A 1 219 ? -20.510 -44.548 22.614  1.00 51.56  ? 219 SER   A O    1 
ATOM   1681 C  CB   . SER   A 1 219 ? -21.610 -42.785 20.301  1.00 57.41  ? 219 SER   A CB   1 
ATOM   1682 O  OG   . SER   A 1 219 ? -20.808 -42.834 19.128  1.00 52.33  ? 219 SER   A OG   1 
ATOM   1683 N  N    . SER   A 1 220 ? -19.914 -45.541 20.646  1.00 48.71  ? 220 SER   A N    1 
ATOM   1684 C  CA   . SER   A 1 220 ? -18.628 -46.144 21.068  1.00 55.29  ? 220 SER   A CA   1 
ATOM   1685 C  C    . SER   A 1 220 ? -17.676 -46.076 19.884  1.00 47.98  ? 220 SER   A C    1 
ATOM   1686 O  O    . SER   A 1 220 ? -18.156 -45.864 18.762  1.00 45.26  ? 220 SER   A O    1 
ATOM   1687 C  CB   . SER   A 1 220 ? -18.773 -47.561 21.593  1.00 55.07  ? 220 SER   A CB   1 
ATOM   1688 O  OG   . SER   A 1 220 ? -19.680 -48.289 20.793  1.00 56.71  ? 220 SER   A OG   1 
ATOM   1689 N  N    . ILE   A 1 221 ? -16.382 -46.156 20.182  1.00 49.41  ? 221 ILE   A N    1 
ATOM   1690 C  CA   . ILE   A 1 221 ? -15.280 -46.022 19.196  1.00 48.85  ? 221 ILE   A CA   1 
ATOM   1691 C  C    . ILE   A 1 221 ? -15.513 -47.111 18.170  1.00 46.15  ? 221 ILE   A C    1 
ATOM   1692 O  O    . ILE   A 1 221 ? -15.509 -48.295 18.505  1.00 41.50  ? 221 ILE   A O    1 
ATOM   1693 C  CB   . ILE   A 1 221 ? -13.904 -46.186 19.866  1.00 46.87  ? 221 ILE   A CB   1 
ATOM   1694 C  CG1  . ILE   A 1 221 ? -13.522 -44.980 20.720  1.00 47.82  ? 221 ILE   A CG1  1 
ATOM   1695 C  CG2  . ILE   A 1 221 ? -12.857 -46.446 18.805  1.00 50.09  ? 221 ILE   A CG2  1 
ATOM   1696 C  CD1  . ILE   A 1 221 ? -12.430 -45.285 21.728  1.00 55.98  ? 221 ILE   A CD1  1 
ATOM   1697 N  N    . PRO   A 1 222 ? -15.837 -46.773 16.914  1.00 46.19  ? 222 PRO   A N    1 
ATOM   1698 C  CA   . PRO   A 1 222 ? -15.968 -47.822 15.905  1.00 45.98  ? 222 PRO   A CA   1 
ATOM   1699 C  C    . PRO   A 1 222 ? -14.605 -48.535 15.770  1.00 50.41  ? 222 PRO   A C    1 
ATOM   1700 O  O    . PRO   A 1 222 ? -13.551 -47.954 16.063  1.00 53.56  ? 222 PRO   A O    1 
ATOM   1701 C  CB   . PRO   A 1 222 ? -16.480 -47.084 14.665  1.00 40.98  ? 222 PRO   A CB   1 
ATOM   1702 C  CG   . PRO   A 1 222 ? -16.192 -45.625 14.914  1.00 41.43  ? 222 PRO   A CG   1 
ATOM   1703 C  CD   . PRO   A 1 222 ? -16.133 -45.434 16.418  1.00 42.76  ? 222 PRO   A CD   1 
ATOM   1704 N  N    . SER   A 1 223 ? -14.646 -49.812 15.421  1.00 49.28  ? 223 SER   A N    1 
ATOM   1705 C  CA   . SER   A 1 223 ? -13.457 -50.680 15.226  1.00 56.50  ? 223 SER   A CA   1 
ATOM   1706 C  C    . SER   A 1 223 ? -12.586 -50.166 14.070  1.00 49.63  ? 223 SER   A C    1 
ATOM   1707 O  O    . SER   A 1 223 ? -13.141 -49.829 13.024  1.00 55.27  ? 223 SER   A O    1 
ATOM   1708 C  CB   . SER   A 1 223 ? -13.893 -52.098 14.981  1.00 64.93  ? 223 SER   A CB   1 
ATOM   1709 O  OG   . SER   A 1 223 ? -12.805 -52.966 15.240  1.00 86.50  ? 223 SER   A OG   1 
ATOM   1710 N  N    . GLY   A 1 224 ? -11.263 -50.126 14.264  1.00 52.78  ? 224 GLY   A N    1 
ATOM   1711 C  CA   . GLY   A 1 224 ? -10.257 -49.666 13.280  1.00 50.36  ? 224 GLY   A CA   1 
ATOM   1712 C  C    . GLY   A 1 224 ? -10.279 -48.157 13.019  1.00 54.65  ? 224 GLY   A C    1 
ATOM   1713 O  O    . GLY   A 1 224 ? -9.815  -47.751 11.940  1.00 60.21  ? 224 GLY   A O    1 
ATOM   1714 N  N    . SER   A 1 225 ? -10.793 -47.327 13.938  1.00 55.11  ? 225 SER   A N    1 
ATOM   1715 C  CA   . SER   A 1 225 ? -10.968 -45.855 13.737  1.00 49.11  ? 225 SER   A CA   1 
ATOM   1716 C  C    . SER   A 1 225 ? -9.757  -45.059 14.275  1.00 45.19  ? 225 SER   A C    1 
ATOM   1717 O  O    . SER   A 1 225 ? -9.867  -43.839 14.482  1.00 46.75  ? 225 SER   A O    1 
ATOM   1718 C  CB   . SER   A 1 225 ? -12.278 -45.373 14.323  1.00 47.97  ? 225 SER   A CB   1 
ATOM   1719 O  OG   . SER   A 1 225 ? -12.269 -45.443 15.742  1.00 44.22  ? 225 SER   A OG   1 
ATOM   1720 N  N    . THR   A 1 226 ? -8.603  -45.695 14.436  1.00 39.02  ? 226 THR   A N    1 
ATOM   1721 C  CA   . THR   A 1 226 ? -7.343  -44.962 14.638  1.00 42.54  ? 226 THR   A CA   1 
ATOM   1722 C  C    . THR   A 1 226 ? -7.016  -44.225 13.347  1.00 39.42  ? 226 THR   A C    1 
ATOM   1723 O  O    . THR   A 1 226 ? -7.720  -44.421 12.371  1.00 37.85  ? 226 THR   A O    1 
ATOM   1724 C  CB   . THR   A 1 226 ? -6.217  -45.917 15.009  1.00 46.85  ? 226 THR   A CB   1 
ATOM   1725 O  OG1  . THR   A 1 226 ? -6.061  -46.748 13.855  1.00 46.74  ? 226 THR   A OG1  1 
ATOM   1726 C  CG2  . THR   A 1 226 ? -6.557  -46.686 16.264  1.00 44.35  ? 226 THR   A CG2  1 
ATOM   1727 N  N    . GLY   A 1 227 ? -5.949  -43.439 13.358  1.00 41.77  ? 227 GLY   A N    1 
ATOM   1728 C  CA   . GLY   A 1 227 ? -5.486  -42.692 12.182  1.00 42.90  ? 227 GLY   A CA   1 
ATOM   1729 C  C    . GLY   A 1 227 ? -6.561  -41.761 11.656  1.00 43.05  ? 227 GLY   A C    1 
ATOM   1730 O  O    . GLY   A 1 227 ? -7.201  -41.082 12.448  1.00 41.12  ? 227 GLY   A O    1 
ATOM   1731 N  N    . ARG   A 1 228 ? -6.766  -41.770 10.348  1.00 42.71  ? 228 ARG   A N    1 
ATOM   1732 C  CA   . ARG   A 1 228 ? -7.491  -40.709 9.602   1.00 41.47  ? 228 ARG   A CA   1 
ATOM   1733 C  C    . ARG   A 1 228 ? -8.979  -40.657 9.951   1.00 37.13  ? 228 ARG   A C    1 
ATOM   1734 O  O    . ARG   A 1 228 ? -9.617  -39.702 9.547   1.00 33.29  ? 228 ARG   A O    1 
ATOM   1735 C  CB   . ARG   A 1 228 ? -7.339  -40.951 8.101   1.00 40.27  ? 228 ARG   A CB   1 
ATOM   1736 C  CG   . ARG   A 1 228 ? -7.882  -42.286 7.621   1.00 37.18  ? 228 ARG   A CG   1 
ATOM   1737 C  CD   . ARG   A 1 228 ? -7.403  -42.525 6.219   1.00 37.59  ? 228 ARG   A CD   1 
ATOM   1738 N  NE   . ARG   A 1 228 ? -8.158  -43.600 5.617   1.00 40.32  ? 228 ARG   A NE   1 
ATOM   1739 C  CZ   . ARG   A 1 228 ? -7.945  -44.063 4.383   1.00 43.24  ? 228 ARG   A CZ   1 
ATOM   1740 N  NH1  . ARG   A 1 228 ? -6.988  -43.568 3.616   1.00 37.72  ? 228 ARG   A NH1  1 
ATOM   1741 N  NH2  . ARG   A 1 228 ? -8.704  -45.023 3.918   1.00 44.97  ? 228 ARG   A NH2  1 
ATOM   1742 N  N    . LEU   A 1 229 ? -9.512  -41.674 10.610  1.00 37.02  ? 229 LEU   A N    1 
ATOM   1743 C  CA   . LEU   A 1 229 ? -10.952 -41.783 10.939  1.00 38.00  ? 229 LEU   A CA   1 
ATOM   1744 C  C    . LEU   A 1 229 ? -11.256 -41.160 12.317  1.00 39.29  ? 229 LEU   A C    1 
ATOM   1745 O  O    . LEU   A 1 229 ? -12.447 -41.086 12.661  1.00 39.21  ? 229 LEU   A O    1 
ATOM   1746 C  CB   . LEU   A 1 229 ? -11.294 -43.272 10.885  1.00 42.48  ? 229 LEU   A CB   1 
ATOM   1747 C  CG   . LEU   A 1 229 ? -11.075 -43.943 9.528   1.00 41.98  ? 229 LEU   A CG   1 
ATOM   1748 C  CD1  . LEU   A 1 229 ? -11.473 -45.412 9.561   1.00 44.12  ? 229 LEU   A CD1  1 
ATOM   1749 C  CD2  . LEU   A 1 229 ? -11.856 -43.243 8.433   1.00 44.93  ? 229 LEU   A CD2  1 
ATOM   1750 N  N    . LEU   A 1 230 ? -10.232 -40.723 13.072  1.00 41.55  ? 230 LEU   A N    1 
ATOM   1751 C  CA   . LEU   A 1 230 ? -10.354 -39.797 14.233  1.00 42.90  ? 230 LEU   A CA   1 
ATOM   1752 C  C    . LEU   A 1 230 ? -11.235 -40.377 15.351  1.00 45.64  ? 230 LEU   A C    1 
ATOM   1753 O  O    . LEU   A 1 230 ? -11.770 -39.587 16.131  1.00 40.18  ? 230 LEU   A O    1 
ATOM   1754 C  CB   . LEU   A 1 230 ? -10.994 -38.494 13.749  1.00 39.48  ? 230 LEU   A CB   1 
ATOM   1755 C  CG   . LEU   A 1 230 ? -10.207 -37.714 12.707  1.00 45.75  ? 230 LEU   A CG   1 
ATOM   1756 C  CD1  . LEU   A 1 230 ? -11.070 -36.614 12.088  1.00 53.34  ? 230 LEU   A CD1  1 
ATOM   1757 C  CD2  . LEU   A 1 230 ? -8.968  -37.126 13.328  1.00 44.68  ? 230 LEU   A CD2  1 
ATOM   1758 N  N    . GLY   A 1 231 ? -11.429 -41.687 15.421  1.00 41.79  ? 231 GLY   A N    1 
ATOM   1759 C  CA   . GLY   A 1 231 ? -12.297 -42.296 16.443  1.00 41.74  ? 231 GLY   A CA   1 
ATOM   1760 C  C    . GLY   A 1 231 ? -13.780 -42.092 16.181  1.00 38.62  ? 231 GLY   A C    1 
ATOM   1761 O  O    . GLY   A 1 231 ? -14.565 -42.369 17.093  1.00 44.09  ? 231 GLY   A O    1 
ATOM   1762 N  N    . LEU   A 1 232 ? -14.171 -41.604 15.011  1.00 34.96  ? 232 LEU   A N    1 
ATOM   1763 C  CA   . LEU   A 1 232 ? -15.572 -41.150 14.765  1.00 41.00  ? 232 LEU   A CA   1 
ATOM   1764 C  C    . LEU   A 1 232 ? -16.285 -42.082 13.780  1.00 45.81  ? 232 LEU   A C    1 
ATOM   1765 O  O    . LEU   A 1 232 ? -17.462 -42.373 14.011  1.00 43.62  ? 232 LEU   A O    1 
ATOM   1766 C  CB   . LEU   A 1 232 ? -15.567 -39.715 14.237  1.00 40.06  ? 232 LEU   A CB   1 
ATOM   1767 C  CG   . LEU   A 1 232 ? -15.002 -38.642 15.177  1.00 44.45  ? 232 LEU   A CG   1 
ATOM   1768 C  CD1  . LEU   A 1 232 ? -15.091 -37.267 14.536  1.00 46.78  ? 232 LEU   A CD1  1 
ATOM   1769 C  CD2  . LEU   A 1 232 ? -15.701 -38.629 16.531  1.00 47.33  ? 232 LEU   A CD2  1 
ATOM   1770 N  N    . PHE   A 1 233 ? -15.579 -42.596 12.768  1.00 48.34  ? 233 PHE   A N    1 
ATOM   1771 C  CA   . PHE   A 1 233 ? -16.180 -43.363 11.662  1.00 47.95  ? 233 PHE   A CA   1 
ATOM   1772 C  C    . PHE   A 1 233 ? -15.626 -44.777 11.560  1.00 44.26  ? 233 PHE   A C    1 
ATOM   1773 O  O    . PHE   A 1 233 ? -14.454 -45.016 11.750  1.00 39.68  ? 233 PHE   A O    1 
ATOM   1774 C  CB   . PHE   A 1 233 ? -15.973 -42.526 10.410  1.00 50.09  ? 233 PHE   A CB   1 
ATOM   1775 C  CG   . PHE   A 1 233 ? -16.703 -41.224 10.546  1.00 48.93  ? 233 PHE   A CG   1 
ATOM   1776 C  CD1  . PHE   A 1 233 ? -18.081 -41.196 10.498  1.00 53.34  ? 233 PHE   A CD1  1 
ATOM   1777 C  CD2  . PHE   A 1 233 ? -16.014 -40.049 10.767  1.00 52.75  ? 233 PHE   A CD2  1 
ATOM   1778 C  CE1  . PHE   A 1 233 ? -18.757 -39.995 10.627  1.00 58.15  ? 233 PHE   A CE1  1 
ATOM   1779 C  CE2  . PHE   A 1 233 ? -16.692 -38.860 10.921  1.00 47.85  ? 233 PHE   A CE2  1 
ATOM   1780 C  CZ   . PHE   A 1 233 ? -18.059 -38.837 10.865  1.00 48.58  ? 233 PHE   A CZ   1 
ATOM   1781 N  N    . PRO   A 1 234 ? -16.449 -45.760 11.144  1.00 53.84  ? 234 PRO   A N    1 
ATOM   1782 C  CA   . PRO   A 1 234 ? -15.932 -47.105 10.865  1.00 53.16  ? 234 PRO   A CA   1 
ATOM   1783 C  C    . PRO   A 1 234 ? -15.114 -47.190 9.556   1.00 50.04  ? 234 PRO   A C    1 
ATOM   1784 O  O    . PRO   A 1 234 ? -14.327 -48.099 9.396   1.00 54.07  ? 234 PRO   A O    1 
ATOM   1785 C  CB   . PRO   A 1 234 ? -17.236 -47.930 10.797  1.00 47.91  ? 234 PRO   A CB   1 
ATOM   1786 C  CG   . PRO   A 1 234 ? -18.273 -46.951 10.270  1.00 48.09  ? 234 PRO   A CG   1 
ATOM   1787 C  CD   . PRO   A 1 234 ? -17.898 -45.614 10.865  1.00 45.60  ? 234 PRO   A CD   1 
ATOM   1788 N  N    . ASP   A 1 235 ? -15.308 -46.242 8.643   1.00 51.07  ? 235 ASP   A N    1 
ATOM   1789 C  CA   . ASP   A 1 235 ? -14.692 -46.268 7.288   1.00 55.25  ? 235 ASP   A CA   1 
ATOM   1790 C  C    . ASP   A 1 235 ? -14.665 -44.845 6.711   1.00 51.30  ? 235 ASP   A C    1 
ATOM   1791 O  O    . ASP   A 1 235 ? -15.268 -43.948 7.326   1.00 55.96  ? 235 ASP   A O    1 
ATOM   1792 C  CB   . ASP   A 1 235 ? -15.454 -47.234 6.369   1.00 55.09  ? 235 ASP   A CB   1 
ATOM   1793 C  CG   . ASP   A 1 235 ? -16.938 -46.918 6.185   1.00 60.35  ? 235 ASP   A CG   1 
ATOM   1794 O  OD1  . ASP   A 1 235 ? -17.289 -45.787 5.727   1.00 55.16  ? 235 ASP   A OD1  1 
ATOM   1795 O  OD2  . ASP   A 1 235 ? -17.748 -47.805 6.495   1.00 71.16  ? 235 ASP   A OD2  1 
ATOM   1796 N  N    . ALA   A 1 236 ? -14.023 -44.661 5.553   1.00 54.65  ? 236 ALA   A N    1 
ATOM   1797 C  CA   . ALA   A 1 236 ? -13.782 -43.337 4.929   1.00 49.08  ? 236 ALA   A CA   1 
ATOM   1798 C  C    . ALA   A 1 236 ? -14.871 -42.962 3.916   1.00 49.81  ? 236 ALA   A C    1 
ATOM   1799 O  O    . ALA   A 1 236 ? -14.625 -42.014 3.176   1.00 58.98  ? 236 ALA   A O    1 
ATOM   1800 C  CB   . ALA   A 1 236 ? -12.419 -43.338 4.276   1.00 54.89  ? 236 ALA   A CB   1 
ATOM   1801 N  N    . ASN   A 1 237 ? -16.008 -43.668 3.845   1.00 51.13  ? 237 ASN   A N    1 
ATOM   1802 C  CA   . ASN   A 1 237 ? -17.124 -43.319 2.921   1.00 59.46  ? 237 ASN   A CA   1 
ATOM   1803 C  C    . ASN   A 1 237 ? -17.714 -41.955 3.261   1.00 65.08  ? 237 ASN   A C    1 
ATOM   1804 O  O    . ASN   A 1 237 ? -17.733 -41.560 4.421   1.00 79.31  ? 237 ASN   A O    1 
ATOM   1805 C  CB   . ASN   A 1 237 ? -18.244 -44.350 2.944   1.00 65.17  ? 237 ASN   A CB   1 
ATOM   1806 C  CG   . ASN   A 1 237 ? -17.782 -45.640 2.314   1.00 68.32  ? 237 ASN   A CG   1 
ATOM   1807 O  OD1  . ASN   A 1 237 ? -16.872 -45.636 1.482   1.00 70.16  ? 237 ASN   A OD1  1 
ATOM   1808 N  ND2  . ASN   A 1 237 ? -18.358 -46.741 2.753   1.00 65.54  ? 237 ASN   A ND2  1 
ATOM   1809 O  OXT  . ASN   A 1 237 ? -18.158 -41.248 2.359   1.00 75.19  ? 237 ASN   A OXT  1 
ATOM   1810 N  N    . ALA   B 1 1   ? -27.849 12.882  13.604  1.00 90.05  ? 1   ALA   B N    1 
ATOM   1811 C  CA   . ALA   B 1 1   ? -28.574 11.665  13.158  1.00 83.47  ? 1   ALA   B CA   1 
ATOM   1812 C  C    . ALA   B 1 1   ? -28.073 10.454  13.963  1.00 79.29  ? 1   ALA   B C    1 
ATOM   1813 O  O    . ALA   B 1 1   ? -26.852 10.168  13.960  1.00 74.96  ? 1   ALA   B O    1 
ATOM   1814 C  CB   . ALA   B 1 1   ? -28.396 11.480  11.665  1.00 85.70  ? 1   ALA   B CB   1 
ATOM   1815 N  N    . ASP   B 1 2   ? -28.983 9.787   14.669  1.00 72.18  ? 2   ASP   B N    1 
ATOM   1816 C  CA   . ASP   B 1 2   ? -28.703 8.525   15.402  1.00 67.30  ? 2   ASP   B CA   1 
ATOM   1817 C  C    . ASP   B 1 2   ? -28.382 7.423   14.383  1.00 64.51  ? 2   ASP   B C    1 
ATOM   1818 O  O    . ASP   B 1 2   ? -28.878 7.488   13.237  1.00 63.65  ? 2   ASP   B O    1 
ATOM   1819 C  CB   . ASP   B 1 2   ? -29.902 8.089   16.257  1.00 73.30  ? 2   ASP   B CB   1 
ATOM   1820 C  CG   . ASP   B 1 2   ? -30.250 8.984   17.438  1.00 68.83  ? 2   ASP   B CG   1 
ATOM   1821 O  OD1  . ASP   B 1 2   ? -29.389 9.797   17.829  1.00 63.35  ? 2   ASP   B OD1  1 
ATOM   1822 O  OD2  . ASP   B 1 2   ? -31.374 8.843   17.968  1.00 76.79  ? 2   ASP   B OD2  1 
ATOM   1823 N  N    . THR   B 1 3   ? -27.580 6.450   14.796  1.00 62.05  ? 3   THR   B N    1 
ATOM   1824 C  CA   . THR   B 1 3   ? -27.354 5.162   14.095  1.00 59.55  ? 3   THR   B CA   1 
ATOM   1825 C  C    . THR   B 1 3   ? -28.183 4.082   14.795  1.00 54.78  ? 3   THR   B C    1 
ATOM   1826 O  O    . THR   B 1 3   ? -27.998 3.894   16.001  1.00 53.94  ? 3   THR   B O    1 
ATOM   1827 C  CB   . THR   B 1 3   ? -25.865 4.825   14.067  1.00 59.93  ? 3   THR   B CB   1 
ATOM   1828 O  OG1  . THR   B 1 3   ? -25.352 5.760   13.124  1.00 70.79  ? 3   THR   B OG1  1 
ATOM   1829 C  CG2  . THR   B 1 3   ? -25.566 3.405   13.649  1.00 68.31  ? 3   THR   B CG2  1 
ATOM   1830 N  N    . ILE   B 1 4   ? -29.051 3.419   14.031  1.00 51.99  ? 4   ILE   B N    1 
ATOM   1831 C  CA   . ILE   B 1 4   ? -30.146 2.534   14.494  1.00 48.39  ? 4   ILE   B CA   1 
ATOM   1832 C  C    . ILE   B 1 4   ? -30.027 1.228   13.720  1.00 52.52  ? 4   ILE   B C    1 
ATOM   1833 O  O    . ILE   B 1 4   ? -29.940 1.281   12.483  1.00 58.21  ? 4   ILE   B O    1 
ATOM   1834 C  CB   . ILE   B 1 4   ? -31.515 3.198   14.264  1.00 52.97  ? 4   ILE   B CB   1 
ATOM   1835 C  CG1  . ILE   B 1 4   ? -31.657 4.493   15.065  1.00 57.18  ? 4   ILE   B CG1  1 
ATOM   1836 C  CG2  . ILE   B 1 4   ? -32.651 2.225   14.584  1.00 60.75  ? 4   ILE   B CG2  1 
ATOM   1837 C  CD1  . ILE   B 1 4   ? -32.064 4.281   16.529  1.00 60.43  ? 4   ILE   B CD1  1 
ATOM   1838 N  N    . VAL   B 1 5   ? -29.950 0.113   14.441  1.00 52.87  ? 5   VAL   B N    1 
ATOM   1839 C  CA   . VAL   B 1 5   ? -30.196 -1.260  13.921  1.00 49.00  ? 5   VAL   B CA   1 
ATOM   1840 C  C    . VAL   B 1 5   ? -31.403 -1.714  14.723  1.00 49.70  ? 5   VAL   B C    1 
ATOM   1841 O  O    . VAL   B 1 5   ? -31.379 -1.450  15.936  1.00 54.35  ? 5   VAL   B O    1 
ATOM   1842 C  CB   . VAL   B 1 5   ? -28.956 -2.142  14.131  1.00 44.94  ? 5   VAL   B CB   1 
ATOM   1843 C  CG1  . VAL   B 1 5   ? -29.230 -3.606  13.858  1.00 48.47  ? 5   VAL   B CG1  1 
ATOM   1844 C  CG2  . VAL   B 1 5   ? -27.791 -1.643  13.294  1.00 48.53  ? 5   VAL   B CG2  1 
ATOM   1845 N  N    . ALA   B 1 6   ? -32.441 -2.263  14.093  1.00 49.28  ? 6   ALA   B N    1 
ATOM   1846 C  CA   . ALA   B 1 6   ? -33.705 -2.567  14.804  1.00 48.34  ? 6   ALA   B CA   1 
ATOM   1847 C  C    . ALA   B 1 6   ? -34.396 -3.811  14.244  1.00 45.41  ? 6   ALA   B C    1 
ATOM   1848 O  O    . ALA   B 1 6   ? -34.319 -4.086  13.047  1.00 48.57  ? 6   ALA   B O    1 
ATOM   1849 C  CB   . ALA   B 1 6   ? -34.612 -1.370  14.786  1.00 44.94  ? 6   ALA   B CB   1 
ATOM   1850 N  N    . VAL   B 1 7   ? -35.072 -4.535  15.123  1.00 46.07  ? 7   VAL   B N    1 
ATOM   1851 C  CA   . VAL   B 1 7   ? -36.066 -5.569  14.727  1.00 51.40  ? 7   VAL   B CA   1 
ATOM   1852 C  C    . VAL   B 1 7   ? -37.466 -5.000  14.971  1.00 47.19  ? 7   VAL   B C    1 
ATOM   1853 O  O    . VAL   B 1 7   ? -37.765 -4.690  16.125  1.00 39.66  ? 7   VAL   B O    1 
ATOM   1854 C  CB   . VAL   B 1 7   ? -35.809 -6.870  15.491  1.00 47.30  ? 7   VAL   B CB   1 
ATOM   1855 C  CG1  . VAL   B 1 7   ? -36.930 -7.866  15.278  1.00 49.47  ? 7   VAL   B CG1  1 
ATOM   1856 C  CG2  . VAL   B 1 7   ? -34.464 -7.459  15.086  1.00 51.03  ? 7   VAL   B CG2  1 
ATOM   1857 N  N    . GLU   B 1 8   ? -38.285 -4.854  13.925  1.00 46.53  ? 8   GLU   B N    1 
ATOM   1858 C  CA   . GLU   B 1 8   ? -39.631 -4.240  14.065  1.00 45.07  ? 8   GLU   B CA   1 
ATOM   1859 C  C    . GLU   B 1 8   ? -40.703 -5.334  14.066  1.00 43.96  ? 8   GLU   B C    1 
ATOM   1860 O  O    . GLU   B 1 8   ? -40.707 -6.183  13.207  1.00 48.38  ? 8   GLU   B O    1 
ATOM   1861 C  CB   . GLU   B 1 8   ? -39.894 -3.148  13.021  1.00 50.17  ? 8   GLU   B CB   1 
ATOM   1862 C  CG   . GLU   B 1 8   ? -39.739 -3.574  11.579  1.00 51.21  ? 8   GLU   B CG   1 
ATOM   1863 C  CD   . GLU   B 1 8   ? -40.362 -2.595  10.593  1.00 49.45  ? 8   GLU   B CD   1 
ATOM   1864 O  OE1  . GLU   B 1 8   ? -39.893 -1.466  10.516  1.00 42.24  ? 8   GLU   B OE1  1 
ATOM   1865 O  OE2  . GLU   B 1 8   ? -41.316 -2.986  9.890   1.00 49.57  ? 8   GLU   B OE2  1 
ATOM   1866 N  N    . LEU   B 1 9   ? -41.521 -5.335  15.099  1.00 46.74  ? 9   LEU   B N    1 
ATOM   1867 C  CA   . LEU   B 1 9   ? -42.865 -5.942  15.124  1.00 55.36  ? 9   LEU   B CA   1 
ATOM   1868 C  C    . LEU   B 1 9   ? -43.802 -4.823  14.636  1.00 52.19  ? 9   LEU   B C    1 
ATOM   1869 O  O    . LEU   B 1 9   ? -44.031 -3.887  15.388  1.00 55.02  ? 9   LEU   B O    1 
ATOM   1870 C  CB   . LEU   B 1 9   ? -43.163 -6.442  16.554  1.00 56.43  ? 9   LEU   B CB   1 
ATOM   1871 C  CG   . LEU   B 1 9   ? -42.464 -7.740  16.989  1.00 54.91  ? 9   LEU   B CG   1 
ATOM   1872 C  CD1  . LEU   B 1 9   ? -40.958 -7.607  16.975  1.00 52.18  ? 9   LEU   B CD1  1 
ATOM   1873 C  CD2  . LEU   B 1 9   ? -42.917 -8.189  18.374  1.00 57.49  ? 9   LEU   B CD2  1 
ATOM   1874 N  N    . ASP   B 1 10  ? -44.188 -4.854  13.365  1.00 49.69  ? 10  ASP   B N    1 
ATOM   1875 C  CA   . ASP   B 1 10  ? -44.881 -3.740  12.669  1.00 50.04  ? 10  ASP   B CA   1 
ATOM   1876 C  C    . ASP   B 1 10  ? -46.327 -4.148  12.398  1.00 42.70  ? 10  ASP   B C    1 
ATOM   1877 O  O    . ASP   B 1 10  ? -46.549 -4.866  11.438  1.00 44.19  ? 10  ASP   B O    1 
ATOM   1878 C  CB   . ASP   B 1 10  ? -44.188 -3.372  11.357  1.00 50.20  ? 10  ASP   B CB   1 
ATOM   1879 C  CG   . ASP   B 1 10  ? -44.766 -2.126  10.706  1.00 48.82  ? 10  ASP   B CG   1 
ATOM   1880 O  OD1  . ASP   B 1 10  ? -45.874 -1.748  11.120  1.00 47.17  ? 10  ASP   B OD1  1 
ATOM   1881 O  OD2  . ASP   B 1 10  ? -44.093 -1.529  9.783   1.00 42.35  ? 10  ASP   B OD2  1 
ATOM   1882 N  N    . THR   B 1 11  ? -47.260 -3.646  13.205  1.00 43.47  ? 11  THR   B N    1 
ATOM   1883 C  CA   . THR   B 1 11  ? -48.682 -4.057  13.241  1.00 43.97  ? 11  THR   B CA   1 
ATOM   1884 C  C    . THR   B 1 11  ? -49.511 -3.383  12.140  1.00 51.76  ? 11  THR   B C    1 
ATOM   1885 O  O    . THR   B 1 11  ? -50.600 -3.925  11.881  1.00 59.53  ? 11  THR   B O    1 
ATOM   1886 C  CB   . THR   B 1 11  ? -49.322 -3.688  14.575  1.00 45.53  ? 11  THR   B CB   1 
ATOM   1887 O  OG1  . THR   B 1 11  ? -49.105 -2.284  14.804  1.00 45.05  ? 11  THR   B OG1  1 
ATOM   1888 C  CG2  . THR   B 1 11  ? -48.781 -4.544  15.701  1.00 44.73  ? 11  THR   B CG2  1 
ATOM   1889 N  N    . TYR   B 1 12  ? -49.029 -2.282  11.530  1.00 52.57  ? 12  TYR   B N    1 
ATOM   1890 C  CA   . TYR   B 1 12  ? -49.790 -1.423  10.575  1.00 48.17  ? 12  TYR   B CA   1 
ATOM   1891 C  C    . TYR   B 1 12  ? -49.047 -1.201  9.250   1.00 42.60  ? 12  TYR   B C    1 
ATOM   1892 O  O    . TYR   B 1 12  ? -48.015 -0.520  9.188   1.00 44.58  ? 12  TYR   B O    1 
ATOM   1893 C  CB   . TYR   B 1 12  ? -50.129 -0.087  11.232  1.00 45.79  ? 12  TYR   B CB   1 
ATOM   1894 C  CG   . TYR   B 1 12  ? -51.006 0.783   10.367  1.00 51.70  ? 12  TYR   B CG   1 
ATOM   1895 C  CD1  . TYR   B 1 12  ? -52.384 0.615   10.349  1.00 51.36  ? 12  TYR   B CD1  1 
ATOM   1896 C  CD2  . TYR   B 1 12  ? -50.449 1.735   9.523   1.00 51.83  ? 12  TYR   B CD2  1 
ATOM   1897 C  CE1  . TYR   B 1 12  ? -53.188 1.383   9.521   1.00 56.60  ? 12  TYR   B CE1  1 
ATOM   1898 C  CE2  . TYR   B 1 12  ? -51.238 2.494   8.672   1.00 52.90  ? 12  TYR   B CE2  1 
ATOM   1899 C  CZ   . TYR   B 1 12  ? -52.614 2.333   8.689   1.00 54.93  ? 12  TYR   B CZ   1 
ATOM   1900 O  OH   . TYR   B 1 12  ? -53.386 3.125   7.894   1.00 53.35  ? 12  TYR   B OH   1 
ATOM   1901 N  N    . PRO   B 1 13  ? -49.582 -1.701  8.117   1.00 45.26  ? 13  PRO   B N    1 
ATOM   1902 C  CA   . PRO   B 1 13  ? -48.931 -1.541  6.815   1.00 46.65  ? 13  PRO   B CA   1 
ATOM   1903 C  C    . PRO   B 1 13  ? -48.972 -0.102  6.316   1.00 47.92  ? 13  PRO   B C    1 
ATOM   1904 O  O    . PRO   B 1 13  ? -50.014 0.360   5.951   1.00 58.34  ? 13  PRO   B O    1 
ATOM   1905 C  CB   . PRO   B 1 13  ? -49.738 -2.429  5.841   1.00 46.69  ? 13  PRO   B CB   1 
ATOM   1906 C  CG   . PRO   B 1 13  ? -50.545 -3.344  6.744   1.00 52.26  ? 13  PRO   B CG   1 
ATOM   1907 C  CD   . PRO   B 1 13  ? -50.800 -2.524  8.003   1.00 54.43  ? 13  PRO   B CD   1 
ATOM   1908 N  N    . ASN   B 1 14  ? -47.835 0.572   6.322   1.00 54.79  ? 14  ASN   B N    1 
ATOM   1909 C  CA   . ASN   B 1 14  ? -47.664 1.859   5.595   1.00 50.53  ? 14  ASN   B CA   1 
ATOM   1910 C  C    . ASN   B 1 14  ? -47.106 1.548   4.200   1.00 55.74  ? 14  ASN   B C    1 
ATOM   1911 O  O    . ASN   B 1 14  ? -45.886 1.606   4.069   1.00 56.77  ? 14  ASN   B O    1 
ATOM   1912 C  CB   . ASN   B 1 14  ? -46.761 2.798   6.389   1.00 48.05  ? 14  ASN   B CB   1 
ATOM   1913 C  CG   . ASN   B 1 14  ? -47.234 2.963   7.819   1.00 49.81  ? 14  ASN   B CG   1 
ATOM   1914 O  OD1  . ASN   B 1 14  ? -46.824 2.217   8.695   1.00 42.98  ? 14  ASN   B OD1  1 
ATOM   1915 N  ND2  . ASN   B 1 14  ? -48.134 3.910   8.049   1.00 55.73  ? 14  ASN   B ND2  1 
ATOM   1916 N  N    . THR   B 1 15  ? -47.957 1.221   3.204   1.00 68.61  ? 15  THR   B N    1 
ATOM   1917 C  CA   . THR   B 1 15  ? -47.529 0.672   1.876   1.00 68.76  ? 15  THR   B CA   1 
ATOM   1918 C  C    . THR   B 1 15  ? -46.781 1.745   1.073   1.00 65.49  ? 15  THR   B C    1 
ATOM   1919 O  O    . THR   B 1 15  ? -45.949 1.343   0.258   1.00 66.17  ? 15  THR   B O    1 
ATOM   1920 C  CB   . THR   B 1 15  ? -48.657 -0.010  1.066   1.00 70.04  ? 15  THR   B CB   1 
ATOM   1921 O  OG1  . THR   B 1 15  ? -49.754 0.847   0.751   1.00 62.54  ? 15  THR   B OG1  1 
ATOM   1922 C  CG2  . THR   B 1 15  ? -49.227 -1.231  1.760   1.00 62.03  ? 15  THR   B CG2  1 
ATOM   1923 N  N    . ASP   B 1 16  ? -46.986 3.034   1.365   1.00 68.01  ? 16  ASP   B N    1 
ATOM   1924 C  CA   . ASP   B 1 16  ? -46.329 4.181   0.671   1.00 74.60  ? 16  ASP   B CA   1 
ATOM   1925 C  C    . ASP   B 1 16  ? -44.823 4.243   0.973   1.00 72.35  ? 16  ASP   B C    1 
ATOM   1926 O  O    . ASP   B 1 16  ? -44.107 4.907   0.195   1.00 79.32  ? 16  ASP   B O    1 
ATOM   1927 C  CB   . ASP   B 1 16  ? -46.978 5.526   1.029   1.00 79.77  ? 16  ASP   B CB   1 
ATOM   1928 C  CG   . ASP   B 1 16  ? -47.365 5.716   2.492   1.00 88.63  ? 16  ASP   B CG   1 
ATOM   1929 O  OD1  . ASP   B 1 16  ? -47.332 4.725   3.251   1.00 90.45  ? 16  ASP   B OD1  1 
ATOM   1930 O  OD2  . ASP   B 1 16  ? -47.740 6.855   2.856   1.00 92.96  ? 16  ASP   B OD2  1 
ATOM   1931 N  N    . ILE   B 1 17  ? -44.359 3.625   2.064   1.00 68.56  ? 17  ILE   B N    1 
ATOM   1932 C  CA   . ILE   B 1 17  ? -42.924 3.635   2.493   1.00 66.97  ? 17  ILE   B CA   1 
ATOM   1933 C  C    . ILE   B 1 17  ? -42.365 2.202   2.554   1.00 61.20  ? 17  ILE   B C    1 
ATOM   1934 O  O    . ILE   B 1 17  ? -41.407 1.978   3.303   1.00 58.45  ? 17  ILE   B O    1 
ATOM   1935 C  CB   . ILE   B 1 17  ? -42.744 4.380   3.836   1.00 63.34  ? 17  ILE   B CB   1 
ATOM   1936 C  CG1  . ILE   B 1 17  ? -43.402 3.648   5.012   1.00 57.88  ? 17  ILE   B CG1  1 
ATOM   1937 C  CG2  . ILE   B 1 17  ? -43.236 5.811   3.703   1.00 61.16  ? 17  ILE   B CG2  1 
ATOM   1938 C  CD1  . ILE   B 1 17  ? -42.876 4.055   6.378   1.00 60.11  ? 17  ILE   B CD1  1 
ATOM   1939 N  N    . GLY   B 1 18  ? -42.918 1.271   1.775   1.00 64.18  ? 18  GLY   B N    1 
ATOM   1940 C  CA   . GLY   B 1 18  ? -42.301 -0.048  1.528   1.00 62.33  ? 18  GLY   B CA   1 
ATOM   1941 C  C    . GLY   B 1 18  ? -42.899 -1.150  2.379   1.00 56.79  ? 18  GLY   B C    1 
ATOM   1942 O  O    . GLY   B 1 18  ? -42.569 -2.308  2.146   1.00 58.48  ? 18  GLY   B O    1 
ATOM   1943 N  N    . ASP   B 1 19  ? -43.754 -0.844  3.347   1.00 53.76  ? 19  ASP   B N    1 
ATOM   1944 C  CA   . ASP   B 1 19  ? -44.307 -1.931  4.196   1.00 57.99  ? 19  ASP   B CA   1 
ATOM   1945 C  C    . ASP   B 1 19  ? -45.028 -2.908  3.266   1.00 64.38  ? 19  ASP   B C    1 
ATOM   1946 O  O    . ASP   B 1 19  ? -45.649 -2.494  2.284   1.00 61.61  ? 19  ASP   B O    1 
ATOM   1947 C  CB   . ASP   B 1 19  ? -45.221 -1.418  5.318   1.00 54.48  ? 19  ASP   B CB   1 
ATOM   1948 C  CG   . ASP   B 1 19  ? -44.495 -0.917  6.559   1.00 53.38  ? 19  ASP   B CG   1 
ATOM   1949 O  OD1  . ASP   B 1 19  ? -43.314 -1.267  6.711   1.00 60.25  ? 19  ASP   B OD1  1 
ATOM   1950 O  OD2  . ASP   B 1 19  ? -45.137 -0.207  7.396   1.00 51.05  ? 19  ASP   B OD2  1 
ATOM   1951 N  N    . PRO   B 1 20  ? -44.979 -4.233  3.535   1.00 65.37  ? 20  PRO   B N    1 
ATOM   1952 C  CA   . PRO   B 1 20  ? -45.886 -5.163  2.868   1.00 65.66  ? 20  PRO   B CA   1 
ATOM   1953 C  C    . PRO   B 1 20  ? -47.331 -4.903  3.337   1.00 68.58  ? 20  PRO   B C    1 
ATOM   1954 O  O    . PRO   B 1 20  ? -47.521 -4.116  4.247   1.00 72.19  ? 20  PRO   B O    1 
ATOM   1955 C  CB   . PRO   B 1 20  ? -45.386 -6.565  3.260   1.00 64.30  ? 20  PRO   B CB   1 
ATOM   1956 C  CG   . PRO   B 1 20  ? -44.286 -6.374  4.301   1.00 58.05  ? 20  PRO   B CG   1 
ATOM   1957 C  CD   . PRO   B 1 20  ? -44.096 -4.889  4.515   1.00 61.45  ? 20  PRO   B CD   1 
ATOM   1958 N  N    . SER   B 1 21  ? -48.299 -5.613  2.752   1.00 71.20  ? 21  SER   B N    1 
ATOM   1959 C  CA   . SER   B 1 21  ? -49.765 -5.379  2.876   1.00 68.03  ? 21  SER   B CA   1 
ATOM   1960 C  C    . SER   B 1 21  ? -50.323 -5.917  4.191   1.00 64.52  ? 21  SER   B C    1 
ATOM   1961 O  O    . SER   B 1 21  ? -51.545 -5.800  4.399   1.00 79.28  ? 21  SER   B O    1 
ATOM   1962 C  CB   . SER   B 1 21  ? -50.513 -6.015  1.727   1.00 68.54  ? 21  SER   B CB   1 
ATOM   1963 O  OG   . SER   B 1 21  ? -50.345 -5.246  0.552   1.00 69.47  ? 21  SER   B OG   1 
ATOM   1964 N  N    . TYR   B 1 22  ? -49.492 -6.495  5.044   1.00 57.42  ? 22  TYR   B N    1 
ATOM   1965 C  CA   . TYR   B 1 22  ? -49.960 -7.230  6.250   1.00 61.66  ? 22  TYR   B CA   1 
ATOM   1966 C  C    . TYR   B 1 22  ? -49.065 -6.903  7.448   1.00 52.39  ? 22  TYR   B C    1 
ATOM   1967 O  O    . TYR   B 1 22  ? -47.918 -6.487  7.279   1.00 49.32  ? 22  TYR   B O    1 
ATOM   1968 C  CB   . TYR   B 1 22  ? -49.988 -8.724  5.921   1.00 61.07  ? 22  TYR   B CB   1 
ATOM   1969 C  CG   . TYR   B 1 22  ? -48.819 -9.145  5.071   1.00 69.01  ? 22  TYR   B CG   1 
ATOM   1970 C  CD1  . TYR   B 1 22  ? -47.516 -8.843  5.452   1.00 79.31  ? 22  TYR   B CD1  1 
ATOM   1971 C  CD2  . TYR   B 1 22  ? -48.998 -9.811  3.875   1.00 72.46  ? 22  TYR   B CD2  1 
ATOM   1972 C  CE1  . TYR   B 1 22  ? -46.427 -9.199  4.676   1.00 77.89  ? 22  TYR   B CE1  1 
ATOM   1973 C  CE2  . TYR   B 1 22  ? -47.919 -10.183 3.088   1.00 73.22  ? 22  TYR   B CE2  1 
ATOM   1974 C  CZ   . TYR   B 1 22  ? -46.629 -9.878  3.489   1.00 75.09  ? 22  TYR   B CZ   1 
ATOM   1975 O  OH   . TYR   B 1 22  ? -45.549 -10.227 2.734   1.00 64.63  ? 22  TYR   B OH   1 
ATOM   1976 N  N    . PRO   B 1 23  ? -49.528 -7.118  8.698   1.00 49.50  ? 23  PRO   B N    1 
ATOM   1977 C  CA   . PRO   B 1 23  ? -48.624 -7.110  9.842   1.00 54.72  ? 23  PRO   B CA   1 
ATOM   1978 C  C    . PRO   B 1 23  ? -47.414 -7.990  9.505   1.00 53.16  ? 23  PRO   B C    1 
ATOM   1979 O  O    . PRO   B 1 23  ? -47.612 -9.082  8.945   1.00 49.06  ? 23  PRO   B O    1 
ATOM   1980 C  CB   . PRO   B 1 23  ? -49.466 -7.709  10.976  1.00 54.94  ? 23  PRO   B CB   1 
ATOM   1981 C  CG   . PRO   B 1 23  ? -50.882 -7.347  10.598  1.00 51.26  ? 23  PRO   B CG   1 
ATOM   1982 C  CD   . PRO   B 1 23  ? -50.899 -7.464  9.089   1.00 50.90  ? 23  PRO   B CD   1 
ATOM   1983 N  N    . HIS   B 1 24  ? -46.218 -7.489  9.812   1.00 44.56  ? 24  HIS   B N    1 
ATOM   1984 C  CA   . HIS   B 1 24  ? -44.933 -8.156  9.503   1.00 49.66  ? 24  HIS   B CA   1 
ATOM   1985 C  C    . HIS   B 1 24  ? -43.898 -7.895  10.612  1.00 49.66  ? 24  HIS   B C    1 
ATOM   1986 O  O    . HIS   B 1 24  ? -44.093 -6.991  11.422  1.00 47.29  ? 24  HIS   B O    1 
ATOM   1987 C  CB   . HIS   B 1 24  ? -44.423 -7.667  8.149   1.00 50.24  ? 24  HIS   B CB   1 
ATOM   1988 C  CG   . HIS   B 1 24  ? -44.364 -6.180  8.090   1.00 50.48  ? 24  HIS   B CG   1 
ATOM   1989 N  ND1  . HIS   B 1 24  ? -45.493 -5.405  7.882   1.00 53.25  ? 24  HIS   B ND1  1 
ATOM   1990 C  CD2  . HIS   B 1 24  ? -43.334 -5.324  8.236   1.00 50.27  ? 24  HIS   B CD2  1 
ATOM   1991 C  CE1  . HIS   B 1 24  ? -45.153 -4.132  7.911   1.00 58.61  ? 24  HIS   B CE1  1 
ATOM   1992 N  NE2  . HIS   B 1 24  ? -43.823 -4.050  8.125   1.00 47.87  ? 24  HIS   B NE2  1 
ATOM   1993 N  N    . ILE   B 1 25  ? -42.819 -8.676  10.609  1.00 49.65  ? 25  ILE   B N    1 
ATOM   1994 C  CA   . ILE   B 1 25  ? -41.554 -8.419  11.354  1.00 50.14  ? 25  ILE   B CA   1 
ATOM   1995 C  C    . ILE   B 1 25  ? -40.471 -8.064  10.333  1.00 45.51  ? 25  ILE   B C    1 
ATOM   1996 O  O    . ILE   B 1 25  ? -40.590 -8.469  9.154   1.00 42.87  ? 25  ILE   B O    1 
ATOM   1997 C  CB   . ILE   B 1 25  ? -41.166 -9.624  12.243  1.00 54.69  ? 25  ILE   B CB   1 
ATOM   1998 C  CG1  . ILE   B 1 25  ? -40.905 -10.890 11.423  1.00 58.94  ? 25  ILE   B CG1  1 
ATOM   1999 C  CG2  . ILE   B 1 25  ? -42.238 -9.858  13.304  1.00 55.29  ? 25  ILE   B CG2  1 
ATOM   2000 C  CD1  . ILE   B 1 25  ? -40.335 -12.041 12.230  1.00 66.47  ? 25  ILE   B CD1  1 
ATOM   2001 N  N    . GLY   B 1 26  ? -39.442 -7.351  10.774  1.00 41.02  ? 26  GLY   B N    1 
ATOM   2002 C  CA   . GLY   B 1 26  ? -38.513 -6.706  9.839   1.00 44.14  ? 26  GLY   B CA   1 
ATOM   2003 C  C    . GLY   B 1 26  ? -37.195 -6.372  10.494  1.00 44.21  ? 26  GLY   B C    1 
ATOM   2004 O  O    . GLY   B 1 26  ? -37.187 -6.047  11.712  1.00 42.58  ? 26  GLY   B O    1 
ATOM   2005 N  N    . ILE   B 1 27  ? -36.123 -6.501  9.710   1.00 43.13  ? 27  ILE   B N    1 
ATOM   2006 C  CA   . ILE   B 1 27  ? -34.761 -6.087  10.114  1.00 47.79  ? 27  ILE   B CA   1 
ATOM   2007 C  C    . ILE   B 1 27  ? -34.455 -4.753  9.442   1.00 48.93  ? 27  ILE   B C    1 
ATOM   2008 O  O    . ILE   B 1 27  ? -34.490 -4.681  8.212   1.00 52.60  ? 27  ILE   B O    1 
ATOM   2009 C  CB   . ILE   B 1 27  ? -33.771 -7.211  9.807   1.00 49.02  ? 27  ILE   B CB   1 
ATOM   2010 C  CG1  . ILE   B 1 27  ? -34.065 -8.384  10.740  1.00 53.96  ? 27  ILE   B CG1  1 
ATOM   2011 C  CG2  . ILE   B 1 27  ? -32.345 -6.713  9.943   1.00 51.50  ? 27  ILE   B CG2  1 
ATOM   2012 C  CD1  . ILE   B 1 27  ? -33.362 -9.645  10.365  1.00 64.82  ? 27  ILE   B CD1  1 
ATOM   2013 N  N    . ASP   B 1 28  ? -34.254 -3.729  10.269  1.00 51.18  ? 28  ASP   B N    1 
ATOM   2014 C  CA   . ASP   B 1 28  ? -34.085 -2.305  9.887   1.00 53.62  ? 28  ASP   B CA   1 
ATOM   2015 C  C    . ASP   B 1 28  ? -32.626 -1.915  10.134  1.00 50.85  ? 28  ASP   B C    1 
ATOM   2016 O  O    . ASP   B 1 28  ? -32.207 -1.896  11.298  1.00 59.00  ? 28  ASP   B O    1 
ATOM   2017 C  CB   . ASP   B 1 28  ? -35.017 -1.398  10.700  1.00 55.04  ? 28  ASP   B CB   1 
ATOM   2018 C  CG   . ASP   B 1 28  ? -36.498 -1.569  10.389  1.00 56.33  ? 28  ASP   B CG   1 
ATOM   2019 O  OD1  . ASP   B 1 28  ? -36.809 -2.220  9.373   1.00 53.43  ? 28  ASP   B OD1  1 
ATOM   2020 O  OD2  . ASP   B 1 28  ? -37.327 -1.049  11.171  1.00 49.13  ? 28  ASP   B OD2  1 
ATOM   2021 N  N    . ILE   B 1 29  ? -31.874 -1.664  9.070   1.00 50.73  ? 29  ILE   B N    1 
ATOM   2022 C  CA   . ILE   B 1 29  ? -30.467 -1.193  9.157   1.00 54.50  ? 29  ILE   B CA   1 
ATOM   2023 C  C    . ILE   B 1 29  ? -30.444 0.260   8.673   1.00 55.17  ? 29  ILE   B C    1 
ATOM   2024 O  O    . ILE   B 1 29  ? -30.348 0.505   7.456   1.00 60.89  ? 29  ILE   B O    1 
ATOM   2025 C  CB   . ILE   B 1 29  ? -29.516 -2.107  8.355   1.00 54.88  ? 29  ILE   B CB   1 
ATOM   2026 C  CG1  . ILE   B 1 29  ? -29.722 -3.597  8.661   1.00 55.08  ? 29  ILE   B CG1  1 
ATOM   2027 C  CG2  . ILE   B 1 29  ? -28.068 -1.667  8.552   1.00 53.36  ? 29  ILE   B CG2  1 
ATOM   2028 C  CD1  . ILE   B 1 29  ? -29.362 -4.029  10.071  1.00 52.77  ? 29  ILE   B CD1  1 
ATOM   2029 N  N    . LYS   B 1 30  ? -30.568 1.185   9.616   1.00 59.54  ? 30  LYS   B N    1 
ATOM   2030 C  CA   . LYS   B 1 30  ? -30.358 2.644   9.422   1.00 62.39  ? 30  LYS   B CA   1 
ATOM   2031 C  C    . LYS   B 1 30  ? -31.515 3.226   8.604   1.00 60.27  ? 30  LYS   B C    1 
ATOM   2032 O  O    . LYS   B 1 30  ? -31.407 4.385   8.193   1.00 66.15  ? 30  LYS   B O    1 
ATOM   2033 C  CB   . LYS   B 1 30  ? -28.998 2.921   8.774   1.00 63.07  ? 30  LYS   B CB   1 
ATOM   2034 C  CG   . LYS   B 1 30  ? -27.808 2.512   9.630   1.00 75.41  ? 30  LYS   B CG   1 
ATOM   2035 C  CD   . LYS   B 1 30  ? -26.472 2.861   9.029   1.00 78.39  ? 30  LYS   B CD   1 
ATOM   2036 C  CE   . LYS   B 1 30  ? -26.170 4.344   9.064   1.00 81.65  ? 30  LYS   B CE   1 
ATOM   2037 N  NZ   . LYS   B 1 30  ? -25.069 4.670   8.128   1.00 85.10  ? 30  LYS   B NZ   1 
ATOM   2038 N  N    . SER   B 1 31  ? -32.614 2.490   8.451   1.00 55.47  ? 31  SER   B N    1 
ATOM   2039 C  CA   . SER   B 1 31  ? -33.799 2.931   7.681   1.00 50.15  ? 31  SER   B CA   1 
ATOM   2040 C  C    . SER   B 1 31  ? -35.059 2.242   8.203   1.00 55.81  ? 31  SER   B C    1 
ATOM   2041 O  O    . SER   B 1 31  ? -34.985 1.015   8.501   1.00 54.58  ? 31  SER   B O    1 
ATOM   2042 C  CB   . SER   B 1 31  ? -33.594 2.656   6.222   1.00 48.81  ? 31  SER   B CB   1 
ATOM   2043 O  OG   . SER   B 1 31  ? -34.834 2.662   5.540   1.00 50.78  ? 31  SER   B OG   1 
ATOM   2044 N  N    . VAL   B 1 32  ? -36.188 2.968   8.223   1.00 50.11  ? 32  VAL   B N    1 
ATOM   2045 C  CA   . VAL   B 1 32  ? -37.526 2.355   8.486   1.00 50.92  ? 32  VAL   B CA   1 
ATOM   2046 C  C    . VAL   B 1 32  ? -37.848 1.342   7.374   1.00 55.18  ? 32  VAL   B C    1 
ATOM   2047 O  O    . VAL   B 1 32  ? -38.707 0.463   7.630   1.00 59.25  ? 32  VAL   B O    1 
ATOM   2048 C  CB   . VAL   B 1 32  ? -38.638 3.409   8.643   1.00 58.64  ? 32  VAL   B CB   1 
ATOM   2049 C  CG1  . VAL   B 1 32  ? -39.019 4.054   7.310   1.00 57.95  ? 32  VAL   B CG1  1 
ATOM   2050 C  CG2  . VAL   B 1 32  ? -39.864 2.842   9.353   1.00 58.28  ? 32  VAL   B CG2  1 
ATOM   2051 N  N    . ARG   B 1 33  ? -37.207 1.450   6.198   1.00 51.28  ? 33  ARG   B N    1 
ATOM   2052 C  CA   . ARG   B 1 33  ? -37.478 0.568   5.030   1.00 52.73  ? 33  ARG   B CA   1 
ATOM   2053 C  C    . ARG   B 1 33  ? -36.726 -0.751  5.244   1.00 54.16  ? 33  ARG   B C    1 
ATOM   2054 O  O    . ARG   B 1 33  ? -35.535 -0.885  4.838   1.00 53.84  ? 33  ARG   B O    1 
ATOM   2055 C  CB   . ARG   B 1 33  ? -37.147 1.257   3.700   1.00 54.83  ? 33  ARG   B CB   1 
ATOM   2056 C  CG   . ARG   B 1 33  ? -38.204 2.257   3.249   1.00 55.88  ? 33  ARG   B CG   1 
ATOM   2057 C  CD   . ARG   B 1 33  ? -37.659 3.197   2.193   1.00 63.62  ? 33  ARG   B CD   1 
ATOM   2058 N  NE   . ARG   B 1 33  ? -38.408 4.446   2.144   1.00 65.69  ? 33  ARG   B NE   1 
ATOM   2059 C  CZ   . ARG   B 1 33  ? -39.478 4.701   1.385   1.00 66.27  ? 33  ARG   B CZ   1 
ATOM   2060 N  NH1  . ARG   B 1 33  ? -39.991 3.788   0.574   1.00 64.47  ? 33  ARG   B NH1  1 
ATOM   2061 N  NH2  . ARG   B 1 33  ? -40.049 5.891   1.456   1.00 63.56  ? 33  ARG   B NH2  1 
ATOM   2062 N  N    . SER   B 1 34  ? -37.398 -1.685  5.905   1.00 47.81  ? 34  SER   B N    1 
ATOM   2063 C  CA   . SER   B 1 34  ? -36.824 -2.996  6.291   1.00 50.72  ? 34  SER   B CA   1 
ATOM   2064 C  C    . SER   B 1 34  ? -36.038 -3.605  5.118   1.00 53.73  ? 34  SER   B C    1 
ATOM   2065 O  O    . SER   B 1 34  ? -36.584 -3.718  4.004   1.00 53.68  ? 34  SER   B O    1 
ATOM   2066 C  CB   . SER   B 1 34  ? -37.903 -3.894  6.801   1.00 47.41  ? 34  SER   B CB   1 
ATOM   2067 O  OG   . SER   B 1 34  ? -38.551 -3.295  7.926   1.00 51.65  ? 34  SER   B OG   1 
ATOM   2068 N  N    . LYS   B 1 35  ? -34.787 -3.987  5.374   1.00 54.22  ? 35  LYS   B N    1 
ATOM   2069 C  CA   . LYS   B 1 35  ? -33.961 -4.784  4.438   1.00 51.68  ? 35  LYS   B CA   1 
ATOM   2070 C  C    . LYS   B 1 35  ? -34.613 -6.152  4.230   1.00 53.62  ? 35  LYS   B C    1 
ATOM   2071 O  O    . LYS   B 1 35  ? -34.366 -6.753  3.170   1.00 52.90  ? 35  LYS   B O    1 
ATOM   2072 C  CB   . LYS   B 1 35  ? -32.542 -4.993  4.968   1.00 53.55  ? 35  LYS   B CB   1 
ATOM   2073 C  CG   . LYS   B 1 35  ? -31.812 -3.736  5.404   1.00 53.00  ? 35  LYS   B CG   1 
ATOM   2074 C  CD   . LYS   B 1 35  ? -31.650 -2.713  4.301   1.00 55.28  ? 35  LYS   B CD   1 
ATOM   2075 C  CE   . LYS   B 1 35  ? -31.009 -1.457  4.836   1.00 55.53  ? 35  LYS   B CE   1 
ATOM   2076 N  NZ   . LYS   B 1 35  ? -30.845 -0.442  3.781   1.00 63.47  ? 35  LYS   B NZ   1 
ATOM   2077 N  N    . LYS   B 1 36  ? -35.394 -6.637  5.198   1.00 48.24  ? 36  LYS   B N    1 
ATOM   2078 C  CA   . LYS   B 1 36  ? -35.998 -7.990  5.124   1.00 50.12  ? 36  LYS   B CA   1 
ATOM   2079 C  C    . LYS   B 1 36  ? -37.244 -8.022  6.016   1.00 47.55  ? 36  LYS   B C    1 
ATOM   2080 O  O    . LYS   B 1 36  ? -37.167 -7.496  7.118   1.00 54.35  ? 36  LYS   B O    1 
ATOM   2081 C  CB   . LYS   B 1 36  ? -34.931 -9.033  5.503   1.00 55.22  ? 36  LYS   B CB   1 
ATOM   2082 C  CG   . LYS   B 1 36  ? -35.294 -10.492 5.219   1.00 58.76  ? 36  LYS   B CG   1 
ATOM   2083 C  CD   . LYS   B 1 36  ? -34.970 -10.974 3.793   1.00 62.00  ? 36  LYS   B CD   1 
ATOM   2084 C  CE   . LYS   B 1 36  ? -34.933 -12.489 3.650   1.00 71.12  ? 36  LYS   B CE   1 
ATOM   2085 N  NZ   . LYS   B 1 36  ? -33.703 -13.088 4.248   1.00 71.20  ? 36  LYS   B NZ   1 
ATOM   2086 N  N    . THR   B 1 37  ? -38.342 -8.638  5.565   1.00 49.41  ? 37  THR   B N    1 
ATOM   2087 C  CA   . THR   B 1 37  ? -39.617 -8.745  6.333   1.00 50.76  ? 37  THR   B CA   1 
ATOM   2088 C  C    . THR   B 1 37  ? -40.172 -10.170 6.241   1.00 44.67  ? 37  THR   B C    1 
ATOM   2089 O  O    . THR   B 1 37  ? -39.688 -10.958 5.445   1.00 47.50  ? 37  THR   B O    1 
ATOM   2090 C  CB   . THR   B 1 37  ? -40.672 -7.719  5.891   1.00 52.54  ? 37  THR   B CB   1 
ATOM   2091 O  OG1  . THR   B 1 37  ? -41.148 -8.081  4.596   1.00 61.11  ? 37  THR   B OG1  1 
ATOM   2092 C  CG2  . THR   B 1 37  ? -40.147 -6.301  5.830   1.00 51.05  ? 37  THR   B CG2  1 
ATOM   2093 N  N    . ALA   B 1 38  ? -41.119 -10.508 7.100   1.00 46.30  ? 38  ALA   B N    1 
ATOM   2094 C  CA   . ALA   B 1 38  ? -41.871 -11.774 7.014   1.00 47.70  ? 38  ALA   B CA   1 
ATOM   2095 C  C    . ALA   B 1 38  ? -43.275 -11.527 7.567   1.00 49.28  ? 38  ALA   B C    1 
ATOM   2096 O  O    . ALA   B 1 38  ? -43.416 -10.777 8.528   1.00 46.99  ? 38  ALA   B O    1 
ATOM   2097 C  CB   . ALA   B 1 38  ? -41.157 -12.879 7.757   1.00 47.38  ? 38  ALA   B CB   1 
ATOM   2098 N  N    . LYS   B 1 39  ? -44.275 -12.130 6.939   1.00 49.11  ? 39  LYS   B N    1 
ATOM   2099 C  CA   . LYS   B 1 39  ? -45.668 -12.089 7.407   1.00 47.78  ? 39  LYS   B CA   1 
ATOM   2100 C  C    . LYS   B 1 39  ? -45.663 -12.474 8.887   1.00 49.57  ? 39  LYS   B C    1 
ATOM   2101 O  O    . LYS   B 1 39  ? -44.883 -13.334 9.299   1.00 52.40  ? 39  LYS   B O    1 
ATOM   2102 C  CB   . LYS   B 1 39  ? -46.528 -13.000 6.528   1.00 56.18  ? 39  LYS   B CB   1 
ATOM   2103 C  CG   . LYS   B 1 39  ? -48.036 -12.814 6.653   1.00 66.44  ? 39  LYS   B CG   1 
ATOM   2104 C  CD   . LYS   B 1 39  ? -48.808 -13.334 5.439   1.00 70.89  ? 39  LYS   B CD   1 
ATOM   2105 C  CE   . LYS   B 1 39  ? -50.309 -13.254 5.618   1.00 77.24  ? 39  LYS   B CE   1 
ATOM   2106 N  NZ   . LYS   B 1 39  ? -50.739 -14.062 6.786   1.00 84.78  ? 39  LYS   B NZ   1 
ATOM   2107 N  N    . TRP   B 1 40  ? -46.542 -11.860 9.653   1.00 51.10  ? 40  TRP   B N    1 
ATOM   2108 C  CA   . TRP   B 1 40  ? -46.659 -12.069 11.106  1.00 53.50  ? 40  TRP   B CA   1 
ATOM   2109 C  C    . TRP   B 1 40  ? -48.128 -11.958 11.472  1.00 51.84  ? 40  TRP   B C    1 
ATOM   2110 O  O    . TRP   B 1 40  ? -48.671 -10.879 11.242  1.00 58.79  ? 40  TRP   B O    1 
ATOM   2111 C  CB   . TRP   B 1 40  ? -45.813 -11.020 11.836  1.00 55.82  ? 40  TRP   B CB   1 
ATOM   2112 C  CG   . TRP   B 1 40  ? -46.008 -11.043 13.314  1.00 54.61  ? 40  TRP   B CG   1 
ATOM   2113 C  CD1  . TRP   B 1 40  ? -46.069 -12.142 14.113  1.00 53.43  ? 40  TRP   B CD1  1 
ATOM   2114 C  CD2  . TRP   B 1 40  ? -46.186 -9.905  14.174  1.00 56.57  ? 40  TRP   B CD2  1 
ATOM   2115 N  NE1  . TRP   B 1 40  ? -46.240 -11.770 15.419  1.00 57.05  ? 40  TRP   B NE1  1 
ATOM   2116 C  CE2  . TRP   B 1 40  ? -46.302 -10.402 15.490  1.00 54.38  ? 40  TRP   B CE2  1 
ATOM   2117 C  CE3  . TRP   B 1 40  ? -46.222 -8.523  13.966  1.00 53.82  ? 40  TRP   B CE3  1 
ATOM   2118 C  CZ2  . TRP   B 1 40  ? -46.468 -9.562  16.587  1.00 54.27  ? 40  TRP   B CZ2  1 
ATOM   2119 C  CZ3  . TRP   B 1 40  ? -46.389 -7.695  15.053  1.00 53.08  ? 40  TRP   B CZ3  1 
ATOM   2120 C  CH2  . TRP   B 1 40  ? -46.494 -8.205  16.347  1.00 49.81  ? 40  TRP   B CH2  1 
ATOM   2121 N  N    . ASN   B 1 41  ? -48.712 -13.027 12.012  1.00 56.62  ? 41  ASN   B N    1 
ATOM   2122 C  CA   . ASN   B 1 41  ? -50.126 -13.086 12.452  1.00 57.33  ? 41  ASN   B CA   1 
ATOM   2123 C  C    . ASN   B 1 41  ? -50.132 -12.689 13.927  1.00 59.02  ? 41  ASN   B C    1 
ATOM   2124 O  O    . ASN   B 1 41  ? -50.247 -13.539 14.814  1.00 62.78  ? 41  ASN   B O    1 
ATOM   2125 C  CB   . ASN   B 1 41  ? -50.770 -14.414 12.054  1.00 63.53  ? 41  ASN   B CB   1 
ATOM   2126 C  CG   . ASN   B 1 41  ? -50.581 -14.691 10.571  1.00 71.55  ? 41  ASN   B CG   1 
ATOM   2127 O  OD1  . ASN   B 1 41  ? -50.987 -13.894 9.720   1.00 73.02  ? 41  ASN   B OD1  1 
ATOM   2128 N  ND2  . ASN   B 1 41  ? -49.927 -15.796 10.245  1.00 66.60  ? 41  ASN   B ND2  1 
ATOM   2129 N  N    . MET   B 1 42  ? -49.926 -11.395 14.128  1.00 65.55  ? 42  MET   B N    1 
ATOM   2130 C  CA   . MET   B 1 42  ? -50.167 -10.658 15.386  1.00 64.18  ? 42  MET   B CA   1 
ATOM   2131 C  C    . MET   B 1 42  ? -51.526 -11.105 15.943  1.00 67.42  ? 42  MET   B C    1 
ATOM   2132 O  O    . MET   B 1 42  ? -52.501 -11.110 15.173  1.00 67.73  ? 42  MET   B O    1 
ATOM   2133 C  CB   . MET   B 1 42  ? -50.165 -9.146  15.114  1.00 58.81  ? 42  MET   B CB   1 
ATOM   2134 C  CG   . MET   B 1 42  ? -49.917 -8.334  16.351  1.00 66.76  ? 42  MET   B CG   1 
ATOM   2135 S  SD   . MET   B 1 42  ? -51.352 -8.188  17.448  1.00 70.42  ? 42  MET   B SD   1 
ATOM   2136 C  CE   . MET   B 1 42  ? -52.312 -7.015  16.486  1.00 74.50  ? 42  MET   B CE   1 
ATOM   2137 N  N    . GLN   B 1 43  ? -51.575 -11.427 17.240  1.00 67.79  ? 43  GLN   B N    1 
ATOM   2138 C  CA   . GLN   B 1 43  ? -52.774 -11.896 17.982  1.00 61.90  ? 43  GLN   B CA   1 
ATOM   2139 C  C    . GLN   B 1 43  ? -53.196 -10.818 18.995  1.00 63.17  ? 43  GLN   B C    1 
ATOM   2140 O  O    . GLN   B 1 43  ? -52.509 -10.603 20.035  1.00 61.03  ? 43  GLN   B O    1 
ATOM   2141 C  CB   . GLN   B 1 43  ? -52.479 -13.250 18.624  1.00 66.75  ? 43  GLN   B CB   1 
ATOM   2142 C  CG   . GLN   B 1 43  ? -52.256 -14.360 17.599  1.00 71.18  ? 43  GLN   B CG   1 
ATOM   2143 C  CD   . GLN   B 1 43  ? -52.265 -15.731 18.239  1.00 77.55  ? 43  GLN   B CD   1 
ATOM   2144 O  OE1  . GLN   B 1 43  ? -52.824 -15.935 19.324  1.00 75.64  ? 43  GLN   B OE1  1 
ATOM   2145 N  NE2  . GLN   B 1 43  ? -51.622 -16.682 17.574  1.00 63.38  ? 43  GLN   B NE2  1 
ATOM   2146 N  N    . ASN   B 1 44  ? -54.299 -10.143 18.687  1.00 62.36  ? 44  ASN   B N    1 
ATOM   2147 C  CA   . ASN   B 1 44  ? -54.814 -9.009  19.484  1.00 63.09  ? 44  ASN   B CA   1 
ATOM   2148 C  C    . ASN   B 1 44  ? -55.017 -9.464  20.932  1.00 57.92  ? 44  ASN   B C    1 
ATOM   2149 O  O    . ASN   B 1 44  ? -55.769 -10.431 21.155  1.00 61.73  ? 44  ASN   B O    1 
ATOM   2150 C  CB   . ASN   B 1 44  ? -56.075 -8.417  18.864  1.00 63.66  ? 44  ASN   B CB   1 
ATOM   2151 C  CG   . ASN   B 1 44  ? -56.171 -6.955  19.209  1.00 68.66  ? 44  ASN   B CG   1 
ATOM   2152 O  OD1  . ASN   B 1 44  ? -56.630 -6.602  20.285  1.00 72.49  ? 44  ASN   B OD1  1 
ATOM   2153 N  ND2  . ASN   B 1 44  ? -55.654 -6.110  18.338  1.00 85.79  ? 44  ASN   B ND2  1 
ATOM   2154 N  N    . GLY   B 1 45  ? -54.313 -8.826  21.867  1.00 55.05  ? 45  GLY   B N    1 
ATOM   2155 C  CA   . GLY   B 1 45  ? -54.525 -9.011  23.316  1.00 54.45  ? 45  GLY   B CA   1 
ATOM   2156 C  C    . GLY   B 1 45  ? -53.876 -10.276 23.864  1.00 49.59  ? 45  GLY   B C    1 
ATOM   2157 O  O    . GLY   B 1 45  ? -54.118 -10.570 25.018  1.00 43.54  ? 45  GLY   B O    1 
ATOM   2158 N  N    . LYS   B 1 46  ? -53.081 -11.004 23.076  1.00 50.68  ? 46  LYS   B N    1 
ATOM   2159 C  CA   . LYS   B 1 46  ? -52.361 -12.216 23.555  1.00 55.37  ? 46  LYS   B CA   1 
ATOM   2160 C  C    . LYS   B 1 46  ? -50.904 -11.847 23.832  1.00 53.20  ? 46  LYS   B C    1 
ATOM   2161 O  O    . LYS   B 1 46  ? -50.334 -11.018 23.111  1.00 59.41  ? 46  LYS   B O    1 
ATOM   2162 C  CB   . LYS   B 1 46  ? -52.463 -13.366 22.548  1.00 62.38  ? 46  LYS   B CB   1 
ATOM   2163 C  CG   . LYS   B 1 46  ? -53.878 -13.784 22.158  1.00 70.45  ? 46  LYS   B CG   1 
ATOM   2164 C  CD   . LYS   B 1 46  ? -54.613 -14.585 23.207  1.00 75.44  ? 46  LYS   B CD   1 
ATOM   2165 C  CE   . LYS   B 1 46  ? -55.958 -15.101 22.728  1.00 83.36  ? 46  LYS   B CE   1 
ATOM   2166 N  NZ   . LYS   B 1 46  ? -56.990 -14.033 22.722  1.00 85.16  ? 46  LYS   B NZ   1 
ATOM   2167 N  N    . VAL   B 1 47  ? -50.320 -12.471 24.845  1.00 57.17  ? 47  VAL   B N    1 
ATOM   2168 C  CA   . VAL   B 1 47  ? -48.868 -12.351 25.183  1.00 52.38  ? 47  VAL   B CA   1 
ATOM   2169 C  C    . VAL   B 1 47  ? -48.003 -13.101 24.146  1.00 50.65  ? 47  VAL   B C    1 
ATOM   2170 O  O    . VAL   B 1 47  ? -48.105 -14.334 24.045  1.00 57.24  ? 47  VAL   B O    1 
ATOM   2171 C  CB   . VAL   B 1 47  ? -48.627 -12.868 26.607  1.00 51.69  ? 47  VAL   B CB   1 
ATOM   2172 C  CG1  . VAL   B 1 47  ? -47.146 -12.885 26.943  1.00 51.09  ? 47  VAL   B CG1  1 
ATOM   2173 C  CG2  . VAL   B 1 47  ? -49.432 -12.058 27.626  1.00 53.68  ? 47  VAL   B CG2  1 
ATOM   2174 N  N    . GLY   B 1 48  ? -47.174 -12.375 23.397  1.00 46.65  ? 48  GLY   B N    1 
ATOM   2175 C  CA   . GLY   B 1 48  ? -46.233 -12.942 22.416  1.00 44.69  ? 48  GLY   B CA   1 
ATOM   2176 C  C    . GLY   B 1 48  ? -44.820 -12.914 22.965  1.00 43.53  ? 48  GLY   B C    1 
ATOM   2177 O  O    . GLY   B 1 48  ? -44.612 -12.265 24.008  1.00 45.63  ? 48  GLY   B O    1 
ATOM   2178 N  N    . THR   B 1 49  ? -43.882 -13.586 22.301  1.00 40.48  ? 49  THR   B N    1 
ATOM   2179 C  CA   . THR   B 1 49  ? -42.453 -13.603 22.700  1.00 43.98  ? 49  THR   B CA   1 
ATOM   2180 C  C    . THR   B 1 49  ? -41.611 -13.292 21.472  1.00 41.82  ? 49  THR   B C    1 
ATOM   2181 O  O    . THR   B 1 49  ? -41.877 -13.913 20.448  1.00 48.03  ? 49  THR   B O    1 
ATOM   2182 C  CB   . THR   B 1 49  ? -42.021 -14.940 23.318  1.00 46.56  ? 49  THR   B CB   1 
ATOM   2183 O  OG1  . THR   B 1 49  ? -42.747 -15.189 24.526  1.00 50.80  ? 49  THR   B OG1  1 
ATOM   2184 C  CG2  . THR   B 1 49  ? -40.549 -14.962 23.646  1.00 44.88  ? 49  THR   B CG2  1 
ATOM   2185 N  N    . ALA   B 1 50  ? -40.633 -12.398 21.624  1.00 38.85  ? 50  ALA   B N    1 
ATOM   2186 C  CA   . ALA   B 1 50  ? -39.617 -12.047 20.615  1.00 43.51  ? 50  ALA   B CA   1 
ATOM   2187 C  C    . ALA   B 1 50  ? -38.243 -12.602 21.031  1.00 46.68  ? 50  ALA   B C    1 
ATOM   2188 O  O    . ALA   B 1 50  ? -37.798 -12.300 22.171  1.00 52.09  ? 50  ALA   B O    1 
ATOM   2189 C  CB   . ALA   B 1 50  ? -39.585 -10.548 20.495  1.00 43.93  ? 50  ALA   B CB   1 
ATOM   2190 N  N    . HIS   B 1 51  ? -37.553 -13.314 20.135  1.00 41.80  ? 51  HIS   B N    1 
ATOM   2191 C  CA   . HIS   B 1 51  ? -36.140 -13.761 20.310  1.00 42.41  ? 51  HIS   B CA   1 
ATOM   2192 C  C    . HIS   B 1 51  ? -35.258 -13.126 19.224  1.00 45.99  ? 51  HIS   B C    1 
ATOM   2193 O  O    . HIS   B 1 51  ? -35.509 -13.349 18.043  1.00 47.96  ? 51  HIS   B O    1 
ATOM   2194 C  CB   . HIS   B 1 51  ? -35.994 -15.288 20.256  1.00 46.30  ? 51  HIS   B CB   1 
ATOM   2195 C  CG   . HIS   B 1 51  ? -36.621 -16.065 21.367  1.00 51.20  ? 51  HIS   B CG   1 
ATOM   2196 N  ND1  . HIS   B 1 51  ? -37.788 -16.819 21.184  1.00 57.00  ? 51  HIS   B ND1  1 
ATOM   2197 C  CD2  . HIS   B 1 51  ? -36.233 -16.268 22.648  1.00 56.48  ? 51  HIS   B CD2  1 
ATOM   2198 C  CE1  . HIS   B 1 51  ? -38.110 -17.412 22.321  1.00 55.44  ? 51  HIS   B CE1  1 
ATOM   2199 N  NE2  . HIS   B 1 51  ? -37.176 -17.081 23.247  1.00 56.93  ? 51  HIS   B NE2  1 
ATOM   2200 N  N    . ILE   B 1 52  ? -34.239 -12.357 19.598  1.00 47.74  ? 52  ILE   B N    1 
ATOM   2201 C  CA   . ILE   B 1 52  ? -33.270 -11.794 18.620  1.00 45.34  ? 52  ILE   B CA   1 
ATOM   2202 C  C    . ILE   B 1 52  ? -31.915 -12.434 18.923  1.00 43.42  ? 52  ILE   B C    1 
ATOM   2203 O  O    . ILE   B 1 52  ? -31.641 -12.598 20.091  1.00 46.43  ? 52  ILE   B O    1 
ATOM   2204 C  CB   . ILE   B 1 52  ? -33.285 -10.259 18.721  1.00 46.66  ? 52  ILE   B CB   1 
ATOM   2205 C  CG1  . ILE   B 1 52  ? -34.672 -9.697  18.395  1.00 46.10  ? 52  ILE   B CG1  1 
ATOM   2206 C  CG2  . ILE   B 1 52  ? -32.224 -9.637  17.828  1.00 47.86  ? 52  ILE   B CG2  1 
ATOM   2207 C  CD1  . ILE   B 1 52  ? -35.394 -9.118  19.563  1.00 47.15  ? 52  ILE   B CD1  1 
ATOM   2208 N  N    . ILE   B 1 53  ? -31.144 -12.844 17.919  1.00 42.63  ? 53  ILE   B N    1 
ATOM   2209 C  CA   . ILE   B 1 53  ? -29.761 -13.396 18.111  1.00 51.89  ? 53  ILE   B CA   1 
ATOM   2210 C  C    . ILE   B 1 53  ? -28.830 -12.838 17.032  1.00 50.06  ? 53  ILE   B C    1 
ATOM   2211 O  O    . ILE   B 1 53  ? -29.250 -12.664 15.877  1.00 49.43  ? 53  ILE   B O    1 
ATOM   2212 C  CB   . ILE   B 1 53  ? -29.720 -14.938 18.120  1.00 52.68  ? 53  ILE   B CB   1 
ATOM   2213 C  CG1  . ILE   B 1 53  ? -30.189 -15.504 16.783  1.00 62.39  ? 53  ILE   B CG1  1 
ATOM   2214 C  CG2  . ILE   B 1 53  ? -30.537 -15.496 19.274  1.00 54.91  ? 53  ILE   B CG2  1 
ATOM   2215 C  CD1  . ILE   B 1 53  ? -30.768 -16.916 16.865  1.00 69.79  ? 53  ILE   B CD1  1 
ATOM   2216 N  N    . TYR   B 1 54  ? -27.588 -12.569 17.395  1.00 47.19  ? 54  TYR   B N    1 
ATOM   2217 C  CA   . TYR   B 1 54  ? -26.539 -12.202 16.419  1.00 46.32  ? 54  TYR   B CA   1 
ATOM   2218 C  C    . TYR   B 1 54  ? -25.261 -12.883 16.869  1.00 46.74  ? 54  TYR   B C    1 
ATOM   2219 O  O    . TYR   B 1 54  ? -24.993 -12.856 18.074  1.00 42.51  ? 54  TYR   B O    1 
ATOM   2220 C  CB   . TYR   B 1 54  ? -26.373 -10.689 16.349  1.00 45.25  ? 54  TYR   B CB   1 
ATOM   2221 C  CG   . TYR   B 1 54  ? -25.294 -10.229 15.401  1.00 53.99  ? 54  TYR   B CG   1 
ATOM   2222 C  CD1  . TYR   B 1 54  ? -25.539 -10.079 14.039  1.00 56.16  ? 54  TYR   B CD1  1 
ATOM   2223 C  CD2  . TYR   B 1 54  ? -24.024 -9.916  15.860  1.00 48.82  ? 54  TYR   B CD2  1 
ATOM   2224 C  CE1  . TYR   B 1 54  ? -24.544 -9.663  13.163  1.00 52.20  ? 54  TYR   B CE1  1 
ATOM   2225 C  CE2  . TYR   B 1 54  ? -23.027 -9.478  15.001  1.00 49.40  ? 54  TYR   B CE2  1 
ATOM   2226 C  CZ   . TYR   B 1 54  ? -23.284 -9.351  13.648  1.00 53.14  ? 54  TYR   B CZ   1 
ATOM   2227 O  OH   . TYR   B 1 54  ? -22.294 -8.906  12.821  1.00 54.41  ? 54  TYR   B OH   1 
ATOM   2228 N  N    . ASN   B 1 55  ? -24.492 -13.455 15.952  1.00 46.76  ? 55  ASN   B N    1 
ATOM   2229 C  CA   . ASN   B 1 55  ? -23.086 -13.770 16.291  1.00 50.70  ? 55  ASN   B CA   1 
ATOM   2230 C  C    . ASN   B 1 55  ? -22.210 -13.249 15.151  1.00 52.43  ? 55  ASN   B C    1 
ATOM   2231 O  O    . ASN   B 1 55  ? -22.701 -13.117 14.010  1.00 42.74  ? 55  ASN   B O    1 
ATOM   2232 C  CB   . ASN   B 1 55  ? -22.899 -15.219 16.734  1.00 51.69  ? 55  ASN   B CB   1 
ATOM   2233 C  CG   . ASN   B 1 55  ? -23.040 -16.195 15.598  1.00 58.86  ? 55  ASN   B CG   1 
ATOM   2234 O  OD1  . ASN   B 1 55  ? -22.460 -15.995 14.535  1.00 71.89  ? 55  ASN   B OD1  1 
ATOM   2235 N  ND2  . ASN   B 1 55  ? -23.812 -17.243 15.823  1.00 66.83  ? 55  ASN   B ND2  1 
ATOM   2236 N  N    . SER   B 1 56  ? -21.006 -12.817 15.525  1.00 54.99  ? 56  SER   B N    1 
ATOM   2237 C  CA   . SER   B 1 56  ? -19.995 -12.207 14.635  1.00 56.11  ? 56  SER   B CA   1 
ATOM   2238 C  C    . SER   B 1 56  ? -19.429 -13.276 13.713  1.00 53.02  ? 56  SER   B C    1 
ATOM   2239 O  O    . SER   B 1 56  ? -18.721 -12.875 12.787  1.00 56.05  ? 56  SER   B O    1 
ATOM   2240 C  CB   . SER   B 1 56  ? -18.891 -11.589 15.416  1.00 51.69  ? 56  SER   B CB   1 
ATOM   2241 O  OG   . SER   B 1 56  ? -18.094 -12.619 15.978  1.00 59.01  ? 56  SER   B OG   1 
ATOM   2242 N  N    . VAL   B 1 57  ? -19.688 -14.564 13.984  1.00 51.59  ? 57  VAL   B N    1 
ATOM   2243 C  CA   . VAL   B 1 57  ? -19.115 -15.669 13.165  1.00 55.53  ? 57  VAL   B CA   1 
ATOM   2244 C  C    . VAL   B 1 57  ? -19.954 -15.797 11.882  1.00 57.04  ? 57  VAL   B C    1 
ATOM   2245 O  O    . VAL   B 1 57  ? -19.367 -15.686 10.822  1.00 64.66  ? 57  VAL   B O    1 
ATOM   2246 C  CB   . VAL   B 1 57  ? -18.973 -16.974 13.967  1.00 57.89  ? 57  VAL   B CB   1 
ATOM   2247 C  CG1  . VAL   B 1 57  ? -18.321 -18.087 13.157  1.00 53.21  ? 57  VAL   B CG1  1 
ATOM   2248 C  CG2  . VAL   B 1 57  ? -18.175 -16.723 15.239  1.00 61.08  ? 57  VAL   B CG2  1 
ATOM   2249 N  N    . ASP   B 1 58  ? -21.279 -15.905 11.961  1.00 61.07  ? 58  ASP   B N    1 
ATOM   2250 C  CA   . ASP   B 1 58  ? -22.172 -15.951 10.766  1.00 64.18  ? 58  ASP   B CA   1 
ATOM   2251 C  C    . ASP   B 1 58  ? -22.545 -14.550 10.280  1.00 60.76  ? 58  ASP   B C    1 
ATOM   2252 O  O    . ASP   B 1 58  ? -23.117 -14.467 9.193   1.00 56.76  ? 58  ASP   B O    1 
ATOM   2253 C  CB   . ASP   B 1 58  ? -23.480 -16.667 11.068  1.00 64.62  ? 58  ASP   B CB   1 
ATOM   2254 C  CG   . ASP   B 1 58  ? -23.236 -17.940 11.840  1.00 73.19  ? 58  ASP   B CG   1 
ATOM   2255 O  OD1  . ASP   B 1 58  ? -22.271 -18.647 11.456  1.00 69.22  ? 58  ASP   B OD1  1 
ATOM   2256 O  OD2  . ASP   B 1 58  ? -23.989 -18.194 12.822  1.00 85.77  ? 58  ASP   B OD2  1 
ATOM   2257 N  N    . LYS   B 1 59  ? -22.298 -13.516 11.090  1.00 64.67  ? 59  LYS   B N    1 
ATOM   2258 C  CA   . LYS   B 1 59  ? -22.629 -12.102 10.780  1.00 67.35  ? 59  LYS   B CA   1 
ATOM   2259 C  C    . LYS   B 1 59  ? -24.097 -12.072 10.322  1.00 66.12  ? 59  LYS   B C    1 
ATOM   2260 O  O    . LYS   B 1 59  ? -24.380 -11.508 9.253   1.00 71.39  ? 59  LYS   B O    1 
ATOM   2261 C  CB   . LYS   B 1 59  ? -21.609 -11.553 9.771   1.00 63.47  ? 59  LYS   B CB   1 
ATOM   2262 C  CG   . LYS   B 1 59  ? -20.156 -11.634 10.233  1.00 74.64  ? 59  LYS   B CG   1 
ATOM   2263 C  CD   . LYS   B 1 59  ? -19.110 -10.967 9.340   1.00 87.25  ? 59  LYS   B CD   1 
ATOM   2264 C  CE   . LYS   B 1 59  ? -19.130 -11.375 7.871   1.00 101.66 ? 59  LYS   B CE   1 
ATOM   2265 N  NZ   . LYS   B 1 59  ? -18.229 -12.518 7.565   1.00 100.24 ? 59  LYS   B NZ   1 
ATOM   2266 N  N    . ARG   B 1 60  ? -24.988 -12.689 11.109  1.00 60.48  ? 60  ARG   B N    1 
ATOM   2267 C  CA   . ARG   B 1 60  ? -26.399 -12.988 10.742  1.00 58.57  ? 60  ARG   B CA   1 
ATOM   2268 C  C    . ARG   B 1 60  ? -27.343 -12.589 11.877  1.00 54.53  ? 60  ARG   B C    1 
ATOM   2269 O  O    . ARG   B 1 60  ? -27.350 -13.309 12.888  1.00 53.42  ? 60  ARG   B O    1 
ATOM   2270 C  CB   . ARG   B 1 60  ? -26.560 -14.478 10.421  1.00 67.94  ? 60  ARG   B CB   1 
ATOM   2271 C  CG   . ARG   B 1 60  ? -27.867 -14.825 9.724   1.00 76.07  ? 60  ARG   B CG   1 
ATOM   2272 C  CD   . ARG   B 1 60  ? -27.725 -15.848 8.607   1.00 79.61  ? 60  ARG   B CD   1 
ATOM   2273 N  NE   . ARG   B 1 60  ? -28.885 -16.739 8.534   1.00 92.38  ? 60  ARG   B NE   1 
ATOM   2274 C  CZ   . ARG   B 1 60  ? -29.975 -16.559 7.778   1.00 97.21  ? 60  ARG   B CZ   1 
ATOM   2275 N  NH1  . ARG   B 1 60  ? -30.950 -17.456 7.816   1.00 97.31  ? 60  ARG   B NH1  1 
ATOM   2276 N  NH2  . ARG   B 1 60  ? -30.095 -15.498 6.992   1.00 86.61  ? 60  ARG   B NH2  1 
ATOM   2277 N  N    . LEU   B 1 61  ? -28.118 -11.506 11.688  1.00 51.33  ? 61  LEU   B N    1 
ATOM   2278 C  CA   . LEU   B 1 61  ? -29.154 -11.018 12.647  1.00 48.61  ? 61  LEU   B CA   1 
ATOM   2279 C  C    . LEU   B 1 61  ? -30.492 -11.707 12.351  1.00 54.22  ? 61  LEU   B C    1 
ATOM   2280 O  O    . LEU   B 1 61  ? -30.997 -11.594 11.194  1.00 53.73  ? 61  LEU   B O    1 
ATOM   2281 C  CB   . LEU   B 1 61  ? -29.287 -9.497  12.527  1.00 48.12  ? 61  LEU   B CB   1 
ATOM   2282 C  CG   . LEU   B 1 61  ? -30.304 -8.836  13.454  1.00 46.00  ? 61  LEU   B CG   1 
ATOM   2283 C  CD1  . LEU   B 1 61  ? -29.986 -9.109  14.921  1.00 48.38  ? 61  LEU   B CD1  1 
ATOM   2284 C  CD2  . LEU   B 1 61  ? -30.326 -7.343  13.200  1.00 49.24  ? 61  LEU   B CD2  1 
ATOM   2285 N  N    . SER   B 1 62  ? -31.056 -12.397 13.345  1.00 44.09  ? 62  SER   B N    1 
ATOM   2286 C  CA   . SER   B 1 62  ? -32.264 -13.225 13.170  1.00 43.43  ? 62  SER   B CA   1 
ATOM   2287 C  C    . SER   B 1 62  ? -33.239 -12.862 14.266  1.00 45.34  ? 62  SER   B C    1 
ATOM   2288 O  O    . SER   B 1 62  ? -32.792 -12.422 15.347  1.00 39.73  ? 62  SER   B O    1 
ATOM   2289 C  CB   . SER   B 1 62  ? -31.940 -14.692 13.176  1.00 52.36  ? 62  SER   B CB   1 
ATOM   2290 O  OG   . SER   B 1 62  ? -31.074 -15.028 12.090  1.00 62.92  ? 62  SER   B OG   1 
ATOM   2291 N  N    . ALA   B 1 63  ? -34.525 -13.014 13.977  1.00 44.65  ? 63  ALA   B N    1 
ATOM   2292 C  CA   . ALA   B 1 63  ? -35.581 -12.782 14.969  1.00 44.01  ? 63  ALA   B CA   1 
ATOM   2293 C  C    . ALA   B 1 63  ? -36.642 -13.853 14.783  1.00 44.05  ? 63  ALA   B C    1 
ATOM   2294 O  O    . ALA   B 1 63  ? -36.872 -14.255 13.660  1.00 49.66  ? 63  ALA   B O    1 
ATOM   2295 C  CB   . ALA   B 1 63  ? -36.138 -11.395 14.814  1.00 45.91  ? 63  ALA   B CB   1 
ATOM   2296 N  N    . VAL   B 1 64  ? -37.236 -14.283 15.883  1.00 44.09  ? 64  VAL   B N    1 
ATOM   2297 C  CA   . VAL   B 1 64  ? -38.360 -15.242 15.928  1.00 45.94  ? 64  VAL   B CA   1 
ATOM   2298 C  C    . VAL   B 1 64  ? -39.404 -14.662 16.886  1.00 44.20  ? 64  VAL   B C    1 
ATOM   2299 O  O    . VAL   B 1 64  ? -39.102 -14.436 18.049  1.00 48.33  ? 64  VAL   B O    1 
ATOM   2300 C  CB   . VAL   B 1 64  ? -37.892 -16.632 16.382  1.00 54.70  ? 64  VAL   B CB   1 
ATOM   2301 C  CG1  . VAL   B 1 64  ? -39.036 -17.620 16.347  1.00 59.96  ? 64  VAL   B CG1  1 
ATOM   2302 C  CG2  . VAL   B 1 64  ? -36.733 -17.144 15.547  1.00 64.92  ? 64  VAL   B CG2  1 
ATOM   2303 N  N    . VAL   B 1 65  ? -40.583 -14.383 16.368  1.00 42.57  ? 65  VAL   B N    1 
ATOM   2304 C  CA   . VAL   B 1 65  ? -41.751 -13.898 17.136  1.00 44.38  ? 65  VAL   B CA   1 
ATOM   2305 C  C    . VAL   B 1 65  ? -42.749 -15.051 17.103  1.00 49.61  ? 65  VAL   B C    1 
ATOM   2306 O  O    . VAL   B 1 65  ? -42.979 -15.641 16.005  1.00 52.74  ? 65  VAL   B O    1 
ATOM   2307 C  CB   . VAL   B 1 65  ? -42.369 -12.628 16.524  1.00 47.06  ? 65  VAL   B CB   1 
ATOM   2308 C  CG1  . VAL   B 1 65  ? -43.546 -12.138 17.357  1.00 46.57  ? 65  VAL   B CG1  1 
ATOM   2309 C  CG2  . VAL   B 1 65  ? -41.341 -11.530 16.319  1.00 48.23  ? 65  VAL   B CG2  1 
ATOM   2310 N  N    . SER   B 1 66  ? -43.339 -15.324 18.249  1.00 44.97  ? 66  SER   B N    1 
ATOM   2311 C  CA   . SER   B 1 66  ? -44.182 -16.503 18.465  1.00 47.63  ? 66  SER   B CA   1 
ATOM   2312 C  C    . SER   B 1 66  ? -45.253 -16.174 19.506  1.00 48.40  ? 66  SER   B C    1 
ATOM   2313 O  O    . SER   B 1 66  ? -45.062 -15.261 20.351  1.00 45.08  ? 66  SER   B O    1 
ATOM   2314 C  CB   . SER   B 1 66  ? -43.308 -17.643 18.881  1.00 49.36  ? 66  SER   B CB   1 
ATOM   2315 O  OG   . SER   B 1 66  ? -42.840 -17.439 20.200  1.00 62.73  ? 66  SER   B OG   1 
ATOM   2316 N  N    . TYR   B 1 67  ? -46.315 -16.961 19.467  1.00 50.03  ? 67  TYR   B N    1 
ATOM   2317 C  CA   . TYR   B 1 67  ? -47.432 -16.976 20.441  1.00 55.23  ? 67  TYR   B CA   1 
ATOM   2318 C  C    . TYR   B 1 67  ? -47.616 -18.440 20.858  1.00 53.82  ? 67  TYR   B C    1 
ATOM   2319 O  O    . TYR   B 1 67  ? -47.328 -19.344 20.061  1.00 47.27  ? 67  TYR   B O    1 
ATOM   2320 C  CB   . TYR   B 1 67  ? -48.666 -16.338 19.777  1.00 53.05  ? 67  TYR   B CB   1 
ATOM   2321 C  CG   . TYR   B 1 67  ? -48.654 -14.835 19.577  1.00 58.08  ? 67  TYR   B CG   1 
ATOM   2322 C  CD1  . TYR   B 1 67  ? -48.917 -13.975 20.635  1.00 58.67  ? 67  TYR   B CD1  1 
ATOM   2323 C  CD2  . TYR   B 1 67  ? -48.456 -14.262 18.326  1.00 54.55  ? 67  TYR   B CD2  1 
ATOM   2324 C  CE1  . TYR   B 1 67  ? -48.971 -12.601 20.460  1.00 55.35  ? 67  TYR   B CE1  1 
ATOM   2325 C  CE2  . TYR   B 1 67  ? -48.472 -12.888 18.142  1.00 49.10  ? 67  TYR   B CE2  1 
ATOM   2326 C  CZ   . TYR   B 1 67  ? -48.749 -12.055 19.211  1.00 54.34  ? 67  TYR   B CZ   1 
ATOM   2327 O  OH   . TYR   B 1 67  ? -48.814 -10.691 19.080  1.00 63.34  ? 67  TYR   B OH   1 
ATOM   2328 N  N    . PRO   B 1 68  ? -48.091 -18.750 22.091  1.00 57.12  ? 68  PRO   B N    1 
ATOM   2329 C  CA   . PRO   B 1 68  ? -48.388 -20.143 22.445  1.00 64.32  ? 68  PRO   B CA   1 
ATOM   2330 C  C    . PRO   B 1 68  ? -49.289 -20.826 21.393  1.00 65.35  ? 68  PRO   B C    1 
ATOM   2331 O  O    . PRO   B 1 68  ? -50.280 -20.247 21.021  1.00 75.81  ? 68  PRO   B O    1 
ATOM   2332 C  CB   . PRO   B 1 68  ? -49.084 -20.043 23.820  1.00 62.53  ? 68  PRO   B CB   1 
ATOM   2333 C  CG   . PRO   B 1 68  ? -48.617 -18.709 24.392  1.00 59.60  ? 68  PRO   B CG   1 
ATOM   2334 C  CD   . PRO   B 1 68  ? -48.391 -17.808 23.187  1.00 57.41  ? 68  PRO   B CD   1 
ATOM   2335 N  N    . ASN   B 1 69  ? -48.891 -22.004 20.901  1.00 69.72  ? 69  ASN   B N    1 
ATOM   2336 C  CA   . ASN   B 1 69  ? -49.735 -22.928 20.092  1.00 76.03  ? 69  ASN   B CA   1 
ATOM   2337 C  C    . ASN   B 1 69  ? -49.965 -22.339 18.705  1.00 77.37  ? 69  ASN   B C    1 
ATOM   2338 O  O    . ASN   B 1 69  ? -51.041 -22.588 18.156  1.00 82.73  ? 69  ASN   B O    1 
ATOM   2339 C  CB   . ASN   B 1 69  ? -51.095 -23.220 20.745  1.00 77.85  ? 69  ASN   B CB   1 
ATOM   2340 C  CG   . ASN   B 1 69  ? -50.985 -23.859 22.118  1.00 86.48  ? 69  ASN   B CG   1 
ATOM   2341 O  OD1  . ASN   B 1 69  ? -51.427 -23.291 23.117  1.00 83.38  ? 69  ASN   B OD1  1 
ATOM   2342 N  ND2  . ASN   B 1 69  ? -50.375 -25.035 22.182  1.00 85.70  ? 69  ASN   B ND2  1 
ATOM   2343 N  N    . ALA   B 1 70  ? -48.998 -21.595 18.165  1.00 76.76  ? 70  ALA   B N    1 
ATOM   2344 C  CA   . ALA   B 1 70  ? -49.089 -20.988 16.817  1.00 73.71  ? 70  ALA   B CA   1 
ATOM   2345 C  C    . ALA   B 1 70  ? -47.771 -21.189 16.076  1.00 71.50  ? 70  ALA   B C    1 
ATOM   2346 O  O    . ALA   B 1 70  ? -46.748 -21.396 16.735  1.00 69.15  ? 70  ALA   B O    1 
ATOM   2347 C  CB   . ALA   B 1 70  ? -49.430 -19.525 16.924  1.00 68.81  ? 70  ALA   B CB   1 
ATOM   2348 N  N    . ASP   B 1 71  ? -47.810 -21.128 14.747  1.00 74.43  ? 71  ASP   B N    1 
ATOM   2349 C  CA   . ASP   B 1 71  ? -46.589 -21.041 13.908  1.00 75.91  ? 71  ASP   B CA   1 
ATOM   2350 C  C    . ASP   B 1 71  ? -45.797 -19.803 14.342  1.00 77.58  ? 71  ASP   B C    1 
ATOM   2351 O  O    . ASP   B 1 71  ? -46.386 -18.839 14.869  1.00 73.40  ? 71  ASP   B O    1 
ATOM   2352 C  CB   . ASP   B 1 71  ? -46.913 -20.948 12.411  1.00 84.00  ? 71  ASP   B CB   1 
ATOM   2353 C  CG   . ASP   B 1 71  ? -47.644 -22.151 11.824  1.00 92.86  ? 71  ASP   B CG   1 
ATOM   2354 O  OD1  . ASP   B 1 71  ? -47.173 -23.293 12.041  1.00 84.48  ? 71  ASP   B OD1  1 
ATOM   2355 O  OD2  . ASP   B 1 71  ? -48.679 -21.937 11.141  1.00 93.38  ? 71  ASP   B OD2  1 
ATOM   2356 N  N    . SER   B 1 72  ? -44.496 -19.825 14.098  1.00 77.33  ? 72  SER   B N    1 
ATOM   2357 C  CA   . SER   B 1 72  ? -43.568 -18.697 14.345  1.00 68.09  ? 72  SER   B CA   1 
ATOM   2358 C  C    . SER   B 1 72  ? -43.426 -17.867 13.069  1.00 63.47  ? 72  SER   B C    1 
ATOM   2359 O  O    . SER   B 1 72  ? -43.461 -18.457 11.976  1.00 69.97  ? 72  SER   B O    1 
ATOM   2360 C  CB   . SER   B 1 72  ? -42.236 -19.240 14.787  1.00 63.24  ? 72  SER   B CB   1 
ATOM   2361 O  OG   . SER   B 1 72  ? -42.376 -19.903 16.031  1.00 70.79  ? 72  SER   B OG   1 
ATOM   2362 N  N    . ALA   B 1 73  ? -43.193 -16.567 13.200  1.00 52.12  ? 73  ALA   B N    1 
ATOM   2363 C  CA   . ALA   B 1 73  ? -42.609 -15.732 12.124  1.00 49.68  ? 73  ALA   B CA   1 
ATOM   2364 C  C    . ALA   B 1 73  ? -41.123 -15.586 12.446  1.00 48.67  ? 73  ALA   B C    1 
ATOM   2365 O  O    . ALA   B 1 73  ? -40.816 -15.359 13.643  1.00 47.76  ? 73  ALA   B O    1 
ATOM   2366 C  CB   . ALA   B 1 73  ? -43.304 -14.389 12.042  1.00 48.33  ? 73  ALA   B CB   1 
ATOM   2367 N  N    . THR   B 1 74  ? -40.247 -15.766 11.454  1.00 45.11  ? 74  THR   B N    1 
ATOM   2368 C  CA   . THR   B 1 74  ? -38.788 -15.575 11.616  1.00 50.48  ? 74  THR   B CA   1 
ATOM   2369 C  C    . THR   B 1 74  ? -38.270 -14.753 10.436  1.00 49.11  ? 74  THR   B C    1 
ATOM   2370 O  O    . THR   B 1 74  ? -38.801 -14.833 9.325   1.00 47.36  ? 74  THR   B O    1 
ATOM   2371 C  CB   . THR   B 1 74  ? -38.022 -16.892 11.854  1.00 58.91  ? 74  THR   B CB   1 
ATOM   2372 O  OG1  . THR   B 1 74  ? -37.297 -17.240 10.681  1.00 57.09  ? 74  THR   B OG1  1 
ATOM   2373 C  CG2  . THR   B 1 74  ? -38.890 -18.062 12.267  1.00 59.21  ? 74  THR   B CG2  1 
ATOM   2374 N  N    . VAL   B 1 75  ? -37.236 -13.980 10.690  1.00 49.20  ? 75  VAL   B N    1 
ATOM   2375 C  CA   . VAL   B 1 75  ? -36.653 -13.071 9.678   1.00 45.82  ? 75  VAL   B CA   1 
ATOM   2376 C  C    . VAL   B 1 75  ? -35.165 -12.982 10.007  1.00 46.79  ? 75  VAL   B C    1 
ATOM   2377 O  O    . VAL   B 1 75  ? -34.805 -13.107 11.206  1.00 53.34  ? 75  VAL   B O    1 
ATOM   2378 C  CB   . VAL   B 1 75  ? -37.419 -11.734 9.696   1.00 49.91  ? 75  VAL   B CB   1 
ATOM   2379 C  CG1  . VAL   B 1 75  ? -37.178 -10.942 10.967  1.00 47.58  ? 75  VAL   B CG1  1 
ATOM   2380 C  CG2  . VAL   B 1 75  ? -37.162 -10.881 8.461   1.00 52.40  ? 75  VAL   B CG2  1 
ATOM   2381 N  N    . SER   B 1 76  ? -34.348 -12.875 8.969   1.00 49.91  ? 76  SER   B N    1 
ATOM   2382 C  CA   . SER   B 1 76  ? -32.879 -13.032 8.995   1.00 54.18  ? 76  SER   B CA   1 
ATOM   2383 C  C    . SER   B 1 76  ? -32.261 -12.147 7.908   1.00 59.95  ? 76  SER   B C    1 
ATOM   2384 O  O    . SER   B 1 76  ? -32.796 -12.096 6.794   1.00 69.87  ? 76  SER   B O    1 
ATOM   2385 C  CB   . SER   B 1 76  ? -32.479 -14.471 8.804   1.00 57.33  ? 76  SER   B CB   1 
ATOM   2386 O  OG   . SER   B 1 76  ? -32.381 -15.165 10.040  1.00 66.45  ? 76  SER   B OG   1 
ATOM   2387 N  N    . TYR   B 1 77  ? -31.145 -11.508 8.232   1.00 59.72  ? 77  TYR   B N    1 
ATOM   2388 C  CA   . TYR   B 1 77  ? -30.363 -10.653 7.327   1.00 57.84  ? 77  TYR   B CA   1 
ATOM   2389 C  C    . TYR   B 1 77  ? -28.878 -10.850 7.635   1.00 60.93  ? 77  TYR   B C    1 
ATOM   2390 O  O    . TYR   B 1 77  ? -28.514 -10.735 8.814   1.00 59.34  ? 77  TYR   B O    1 
ATOM   2391 C  CB   . TYR   B 1 77  ? -30.794 -9.199  7.515   1.00 59.92  ? 77  TYR   B CB   1 
ATOM   2392 C  CG   . TYR   B 1 77  ? -30.291 -8.271  6.438   1.00 57.19  ? 77  TYR   B CG   1 
ATOM   2393 C  CD1  . TYR   B 1 77  ? -30.704 -8.407  5.116   1.00 53.91  ? 77  TYR   B CD1  1 
ATOM   2394 C  CD2  . TYR   B 1 77  ? -29.401 -7.253  6.740   1.00 62.49  ? 77  TYR   B CD2  1 
ATOM   2395 C  CE1  . TYR   B 1 77  ? -30.253 -7.546  4.127   1.00 51.56  ? 77  TYR   B CE1  1 
ATOM   2396 C  CE2  . TYR   B 1 77  ? -28.934 -6.390  5.757   1.00 65.53  ? 77  TYR   B CE2  1 
ATOM   2397 C  CZ   . TYR   B 1 77  ? -29.360 -6.538  4.448   1.00 54.59  ? 77  TYR   B CZ   1 
ATOM   2398 O  OH   . TYR   B 1 77  ? -28.908 -5.668  3.505   1.00 59.26  ? 77  TYR   B OH   1 
ATOM   2399 N  N    . ASP   B 1 78  ? -28.075 -11.095 6.593   1.00 64.35  ? 78  ASP   B N    1 
ATOM   2400 C  CA   . ASP   B 1 78  ? -26.590 -11.136 6.622   1.00 68.45  ? 78  ASP   B CA   1 
ATOM   2401 C  C    . ASP   B 1 78  ? -26.071 -9.706  6.657   1.00 65.22  ? 78  ASP   B C    1 
ATOM   2402 O  O    . ASP   B 1 78  ? -26.167 -9.006  5.648   1.00 80.42  ? 78  ASP   B O    1 
ATOM   2403 C  CB   . ASP   B 1 78  ? -25.995 -11.871 5.419   1.00 69.62  ? 78  ASP   B CB   1 
ATOM   2404 C  CG   . ASP   B 1 78  ? -26.294 -13.354 5.443   1.00 73.14  ? 78  ASP   B CG   1 
ATOM   2405 O  OD1  . ASP   B 1 78  ? -26.380 -13.919 6.560   1.00 88.07  ? 78  ASP   B OD1  1 
ATOM   2406 O  OD2  . ASP   B 1 78  ? -26.448 -13.932 4.358   1.00 75.81  ? 78  ASP   B OD2  1 
ATOM   2407 N  N    . VAL   B 1 79  ? -25.532 -9.314  7.800   1.00 63.82  ? 79  VAL   B N    1 
ATOM   2408 C  CA   . VAL   B 1 79  ? -24.995 -7.952  8.041   1.00 58.86  ? 79  VAL   B CA   1 
ATOM   2409 C  C    . VAL   B 1 79  ? -23.872 -8.094  9.065   1.00 57.36  ? 79  VAL   B C    1 
ATOM   2410 O  O    . VAL   B 1 79  ? -23.975 -8.941  9.975   1.00 56.89  ? 79  VAL   B O    1 
ATOM   2411 C  CB   . VAL   B 1 79  ? -26.094 -6.978  8.508   1.00 60.57  ? 79  VAL   B CB   1 
ATOM   2412 C  CG1  . VAL   B 1 79  ? -26.877 -7.509  9.714   1.00 58.00  ? 79  VAL   B CG1  1 
ATOM   2413 C  CG2  . VAL   B 1 79  ? -25.525 -5.600  8.801   1.00 61.99  ? 79  VAL   B CG2  1 
ATOM   2414 N  N    . ASP   B 1 80  ? -22.822 -7.311  8.861   1.00 60.45  ? 80  ASP   B N    1 
ATOM   2415 C  CA   . ASP   B 1 80  ? -21.642 -7.224  9.741   1.00 59.29  ? 80  ASP   B CA   1 
ATOM   2416 C  C    . ASP   B 1 80  ? -21.813 -5.952  10.563  1.00 58.69  ? 80  ASP   B C    1 
ATOM   2417 O  O    . ASP   B 1 80  ? -21.546 -4.879  10.029  1.00 58.36  ? 80  ASP   B O    1 
ATOM   2418 C  CB   . ASP   B 1 80  ? -20.354 -7.253  8.920   1.00 58.03  ? 80  ASP   B CB   1 
ATOM   2419 C  CG   . ASP   B 1 80  ? -19.129 -7.346  9.807   1.00 65.36  ? 80  ASP   B CG   1 
ATOM   2420 O  OD1  . ASP   B 1 80  ? -19.258 -6.951  10.989  1.00 60.40  ? 80  ASP   B OD1  1 
ATOM   2421 O  OD2  . ASP   B 1 80  ? -18.070 -7.846  9.322   1.00 65.90  ? 80  ASP   B OD2  1 
ATOM   2422 N  N    . LEU   B 1 81  ? -22.242 -6.084  11.815  1.00 60.33  ? 81  LEU   B N    1 
ATOM   2423 C  CA   . LEU   B 1 81  ? -22.710 -4.942  12.634  1.00 56.78  ? 81  LEU   B CA   1 
ATOM   2424 C  C    . LEU   B 1 81  ? -21.526 -4.085  13.092  1.00 63.78  ? 81  LEU   B C    1 
ATOM   2425 O  O    . LEU   B 1 81  ? -21.800 -3.008  13.650  1.00 65.72  ? 81  LEU   B O    1 
ATOM   2426 C  CB   . LEU   B 1 81  ? -23.554 -5.468  13.801  1.00 59.77  ? 81  LEU   B CB   1 
ATOM   2427 C  CG   . LEU   B 1 81  ? -24.891 -6.129  13.423  1.00 63.00  ? 81  LEU   B CG   1 
ATOM   2428 C  CD1  . LEU   B 1 81  ? -25.688 -6.503  14.663  1.00 66.13  ? 81  LEU   B CD1  1 
ATOM   2429 C  CD2  . LEU   B 1 81  ? -25.749 -5.237  12.529  1.00 63.58  ? 81  LEU   B CD2  1 
ATOM   2430 N  N    . ASP   B 1 82  ? -20.267 -4.473  12.830  1.00 73.64  ? 82  ASP   B N    1 
ATOM   2431 C  CA   . ASP   B 1 82  ? -19.117 -3.543  13.067  1.00 77.20  ? 82  ASP   B CA   1 
ATOM   2432 C  C    . ASP   B 1 82  ? -18.906 -2.609  11.857  1.00 72.96  ? 82  ASP   B C    1 
ATOM   2433 O  O    . ASP   B 1 82  ? -18.267 -1.551  12.029  1.00 67.15  ? 82  ASP   B O    1 
ATOM   2434 C  CB   . ASP   B 1 82  ? -17.845 -4.249  13.542  1.00 84.05  ? 82  ASP   B CB   1 
ATOM   2435 C  CG   . ASP   B 1 82  ? -17.474 -5.550  12.860  1.00 95.67  ? 82  ASP   B CG   1 
ATOM   2436 O  OD1  . ASP   B 1 82  ? -16.970 -5.490  11.705  1.00 100.32 ? 82  ASP   B OD1  1 
ATOM   2437 O  OD2  . ASP   B 1 82  ? -17.646 -6.609  13.520  1.00 75.26  ? 82  ASP   B OD2  1 
ATOM   2438 N  N    . ASN   B 1 83  ? -19.512 -2.898  10.704  1.00 65.55  ? 83  ASN   B N    1 
ATOM   2439 C  CA   . ASN   B 1 83  ? -19.549 -1.948  9.561   1.00 67.74  ? 83  ASN   B CA   1 
ATOM   2440 C  C    . ASN   B 1 83  ? -20.717 -0.966  9.733   1.00 63.54  ? 83  ASN   B C    1 
ATOM   2441 O  O    . ASN   B 1 83  ? -20.715 0.048   9.018   1.00 68.61  ? 83  ASN   B O    1 
ATOM   2442 C  CB   . ASN   B 1 83  ? -19.568 -2.685  8.216   1.00 72.72  ? 83  ASN   B CB   1 
ATOM   2443 C  CG   . ASN   B 1 83  ? -18.345 -3.563  8.000   1.00 77.93  ? 83  ASN   B CG   1 
ATOM   2444 O  OD1  . ASN   B 1 83  ? -17.334 -3.426  8.695   1.00 73.92  ? 83  ASN   B OD1  1 
ATOM   2445 N  ND2  . ASN   B 1 83  ? -18.421 -4.470  7.038   1.00 77.45  ? 83  ASN   B ND2  1 
ATOM   2446 N  N    . VAL   B 1 84  ? -21.654 -1.224  10.655  1.00 64.17  ? 84  VAL   B N    1 
ATOM   2447 C  CA   . VAL   B 1 84  ? -22.893 -0.406  10.864  1.00 64.22  ? 84  VAL   B CA   1 
ATOM   2448 C  C    . VAL   B 1 84  ? -22.854 0.342   12.211  1.00 61.40  ? 84  VAL   B C    1 
ATOM   2449 O  O    . VAL   B 1 84  ? -23.103 1.565   12.213  1.00 63.50  ? 84  VAL   B O    1 
ATOM   2450 C  CB   . VAL   B 1 84  ? -24.164 -1.274  10.775  1.00 66.75  ? 84  VAL   B CB   1 
ATOM   2451 C  CG1  . VAL   B 1 84  ? -25.399 -0.413  10.640  1.00 68.43  ? 84  VAL   B CG1  1 
ATOM   2452 C  CG2  . VAL   B 1 84  ? -24.108 -2.283  9.641   1.00 69.84  ? 84  VAL   B CG2  1 
ATOM   2453 N  N    . LEU   B 1 85  ? -22.654 -0.361  13.334  1.00 60.86  ? 85  LEU   B N    1 
ATOM   2454 C  CA   . LEU   B 1 85  ? -22.734 0.222   14.709  1.00 56.90  ? 85  LEU   B CA   1 
ATOM   2455 C  C    . LEU   B 1 85  ? -21.364 0.750   15.176  1.00 54.15  ? 85  LEU   B C    1 
ATOM   2456 O  O    . LEU   B 1 85  ? -20.322 0.195   14.841  1.00 59.44  ? 85  LEU   B O    1 
ATOM   2457 C  CB   . LEU   B 1 85  ? -23.307 -0.849  15.653  1.00 58.71  ? 85  LEU   B CB   1 
ATOM   2458 C  CG   . LEU   B 1 85  ? -24.764 -1.274  15.403  1.00 57.95  ? 85  LEU   B CG   1 
ATOM   2459 C  CD1  . LEU   B 1 85  ? -25.138 -2.509  16.217  1.00 61.99  ? 85  LEU   B CD1  1 
ATOM   2460 C  CD2  . LEU   B 1 85  ? -25.730 -0.148  15.731  1.00 54.51  ? 85  LEU   B CD2  1 
ATOM   2461 N  N    . PRO   B 1 86  ? -21.289 1.844   15.973  1.00 55.97  ? 86  PRO   B N    1 
ATOM   2462 C  CA   . PRO   B 1 86  ? -20.069 2.152   16.731  1.00 55.41  ? 86  PRO   B CA   1 
ATOM   2463 C  C    . PRO   B 1 86  ? -19.758 1.054   17.771  1.00 62.30  ? 86  PRO   B C    1 
ATOM   2464 O  O    . PRO   B 1 86  ? -20.658 0.289   18.112  1.00 64.01  ? 86  PRO   B O    1 
ATOM   2465 C  CB   . PRO   B 1 86  ? -20.410 3.461   17.452  1.00 53.61  ? 86  PRO   B CB   1 
ATOM   2466 C  CG   . PRO   B 1 86  ? -21.930 3.460   17.538  1.00 58.83  ? 86  PRO   B CG   1 
ATOM   2467 C  CD   . PRO   B 1 86  ? -22.391 2.782   16.267  1.00 55.94  ? 86  PRO   B CD   1 
ATOM   2468 N  N    . GLU   B 1 87  ? -18.516 0.964   18.254  1.00 63.20  ? 87  GLU   B N    1 
ATOM   2469 C  CA   . GLU   B 1 87  ? -18.087 -0.117  19.192  1.00 64.40  ? 87  GLU   B CA   1 
ATOM   2470 C  C    . GLU   B 1 87  ? -19.018 -0.138  20.413  1.00 57.32  ? 87  GLU   B C    1 
ATOM   2471 O  O    . GLU   B 1 87  ? -19.349 -1.253  20.892  1.00 53.28  ? 87  GLU   B O    1 
ATOM   2472 C  CB   . GLU   B 1 87  ? -16.635 0.079   19.645  1.00 73.85  ? 87  GLU   B CB   1 
ATOM   2473 C  CG   . GLU   B 1 87  ? -15.600 -0.600  18.754  1.00 85.82  ? 87  GLU   B CG   1 
ATOM   2474 C  CD   . GLU   B 1 87  ? -14.229 -0.836  19.382  1.00 86.05  ? 87  GLU   B CD   1 
ATOM   2475 O  OE1  . GLU   B 1 87  ? -14.169 -1.137  20.582  1.00 67.89  ? 87  GLU   B OE1  1 
ATOM   2476 O  OE2  . GLU   B 1 87  ? -13.217 -0.754  18.655  1.00 101.70 ? 87  GLU   B OE2  1 
ATOM   2477 N  N    . TRP   B 1 88  ? -19.403 1.044   20.916  1.00 52.50  ? 88  TRP   B N    1 
ATOM   2478 C  CA   . TRP   B 1 88  ? -20.226 1.195   22.146  1.00 53.92  ? 88  TRP   B CA   1 
ATOM   2479 C  C    . TRP   B 1 88  ? -21.630 1.678   21.782  1.00 53.54  ? 88  TRP   B C    1 
ATOM   2480 O  O    . TRP   B 1 88  ? -21.745 2.608   20.955  1.00 59.29  ? 88  TRP   B O    1 
ATOM   2481 C  CB   . TRP   B 1 88  ? -19.540 2.104   23.171  1.00 50.72  ? 88  TRP   B CB   1 
ATOM   2482 C  CG   . TRP   B 1 88  ? -18.290 1.517   23.776  1.00 53.56  ? 88  TRP   B CG   1 
ATOM   2483 C  CD1  . TRP   B 1 88  ? -17.018 1.652   23.304  1.00 54.45  ? 88  TRP   B CD1  1 
ATOM   2484 C  CD2  . TRP   B 1 88  ? -18.173 0.725   24.976  1.00 48.65  ? 88  TRP   B CD2  1 
ATOM   2485 N  NE1  . TRP   B 1 88  ? -16.128 1.008   24.117  1.00 53.54  ? 88  TRP   B NE1  1 
ATOM   2486 C  CE2  . TRP   B 1 88  ? -16.806 0.434   25.153  1.00 48.53  ? 88  TRP   B CE2  1 
ATOM   2487 C  CE3  . TRP   B 1 88  ? -19.085 0.219   25.913  1.00 52.10  ? 88  TRP   B CE3  1 
ATOM   2488 C  CZ2  . TRP   B 1 88  ? -16.334 -0.330  26.221  1.00 51.25  ? 88  TRP   B CZ2  1 
ATOM   2489 C  CZ3  . TRP   B 1 88  ? -18.621 -0.541  26.970  1.00 48.85  ? 88  TRP   B CZ3  1 
ATOM   2490 C  CH2  . TRP   B 1 88  ? -17.260 -0.802  27.128  1.00 50.73  ? 88  TRP   B CH2  1 
ATOM   2491 N  N    . VAL   B 1 89  ? -22.648 1.042   22.375  1.00 49.76  ? 89  VAL   B N    1 
ATOM   2492 C  CA   . VAL   B 1 89  ? -24.086 1.246   22.040  1.00 51.24  ? 89  VAL   B CA   1 
ATOM   2493 C  C    . VAL   B 1 89  ? -24.928 1.241   23.332  1.00 54.36  ? 89  VAL   B C    1 
ATOM   2494 O  O    . VAL   B 1 89  ? -24.430 0.740   24.380  1.00 52.27  ? 89  VAL   B O    1 
ATOM   2495 C  CB   . VAL   B 1 89  ? -24.583 0.145   21.076  1.00 49.06  ? 89  VAL   B CB   1 
ATOM   2496 C  CG1  . VAL   B 1 89  ? -23.849 0.129   19.756  1.00 53.25  ? 89  VAL   B CG1  1 
ATOM   2497 C  CG2  . VAL   B 1 89  ? -24.502 -1.221  21.710  1.00 50.81  ? 89  VAL   B CG2  1 
ATOM   2498 N  N    . ARG   B 1 90  ? -26.178 1.722   23.242  1.00 42.98  ? 90  ARG   B N    1 
ATOM   2499 C  CA   . ARG   B 1 90  ? -27.258 1.316   24.162  1.00 44.43  ? 90  ARG   B CA   1 
ATOM   2500 C  C    . ARG   B 1 90  ? -28.224 0.389   23.422  1.00 42.86  ? 90  ARG   B C    1 
ATOM   2501 O  O    . ARG   B 1 90  ? -28.282 0.447   22.198  1.00 43.67  ? 90  ARG   B O    1 
ATOM   2502 C  CB   . ARG   B 1 90  ? -27.962 2.525   24.781  1.00 47.93  ? 90  ARG   B CB   1 
ATOM   2503 C  CG   . ARG   B 1 90  ? -27.108 3.241   25.823  1.00 50.42  ? 90  ARG   B CG   1 
ATOM   2504 C  CD   . ARG   B 1 90  ? -27.940 4.140   26.688  1.00 54.53  ? 90  ARG   B CD   1 
ATOM   2505 N  NE   . ARG   B 1 90  ? -27.299 4.478   27.957  1.00 59.40  ? 90  ARG   B NE   1 
ATOM   2506 C  CZ   . ARG   B 1 90  ? -26.714 5.644   28.242  1.00 55.00  ? 90  ARG   B CZ   1 
ATOM   2507 N  NH1  . ARG   B 1 90  ? -26.646 6.611   27.336  1.00 57.60  ? 90  ARG   B NH1  1 
ATOM   2508 N  NH2  . ARG   B 1 90  ? -26.182 5.828   29.437  1.00 47.23  ? 90  ARG   B NH2  1 
ATOM   2509 N  N    . VAL   B 1 91  ? -28.943 -0.449  24.171  1.00 40.90  ? 91  VAL   B N    1 
ATOM   2510 C  CA   . VAL   B 1 91  ? -30.016 -1.322  23.645  1.00 40.92  ? 91  VAL   B CA   1 
ATOM   2511 C  C    . VAL   B 1 91  ? -31.328 -0.844  24.248  1.00 44.16  ? 91  VAL   B C    1 
ATOM   2512 O  O    . VAL   B 1 91  ? -31.298 -0.283  25.369  1.00 40.07  ? 91  VAL   B O    1 
ATOM   2513 C  CB   . VAL   B 1 91  ? -29.720 -2.791  23.961  1.00 45.25  ? 91  VAL   B CB   1 
ATOM   2514 C  CG1  . VAL   B 1 91  ? -28.356 -3.160  23.397  1.00 48.55  ? 91  VAL   B CG1  1 
ATOM   2515 C  CG2  . VAL   B 1 91  ? -29.831 -3.110  25.448  1.00 45.92  ? 91  VAL   B CG2  1 
ATOM   2516 N  N    . GLY   B 1 92  ? -32.432 -1.048  23.528  1.00 43.84  ? 92  GLY   B N    1 
ATOM   2517 C  CA   . GLY   B 1 92  ? -33.713 -0.451  23.927  1.00 42.19  ? 92  GLY   B CA   1 
ATOM   2518 C  C    . GLY   B 1 92  ? -34.900 -1.103  23.262  1.00 42.05  ? 92  GLY   B C    1 
ATOM   2519 O  O    . GLY   B 1 92  ? -34.734 -1.978  22.390  1.00 40.00  ? 92  GLY   B O    1 
ATOM   2520 N  N    . LEU   B 1 93  ? -36.069 -0.697  23.736  1.00 45.46  ? 93  LEU   B N    1 
ATOM   2521 C  CA   . LEU   B 1 93  ? -37.392 -0.985  23.142  1.00 45.35  ? 93  LEU   B CA   1 
ATOM   2522 C  C    . LEU   B 1 93  ? -38.091 0.352   22.831  1.00 48.11  ? 93  LEU   B C    1 
ATOM   2523 O  O    . LEU   B 1 93  ? -38.038 1.294   23.625  1.00 44.60  ? 93  LEU   B O    1 
ATOM   2524 C  CB   . LEU   B 1 93  ? -38.184 -1.838  24.136  1.00 44.64  ? 93  LEU   B CB   1 
ATOM   2525 C  CG   . LEU   B 1 93  ? -37.488 -3.101  24.656  1.00 45.42  ? 93  LEU   B CG   1 
ATOM   2526 C  CD1  . LEU   B 1 93  ? -38.424 -3.878  25.561  1.00 46.95  ? 93  LEU   B CD1  1 
ATOM   2527 C  CD2  . LEU   B 1 93  ? -37.002 -3.989  23.532  1.00 46.39  ? 93  LEU   B CD2  1 
ATOM   2528 N  N    . SER   B 1 94  ? -38.666 0.443   21.654  1.00 46.59  ? 94  SER   B N    1 
ATOM   2529 C  CA   . SER   B 1 94  ? -39.414 1.610   21.166  1.00 46.13  ? 94  SER   B CA   1 
ATOM   2530 C  C    . SER   B 1 94  ? -40.811 1.139   20.780  1.00 45.88  ? 94  SER   B C    1 
ATOM   2531 O  O    . SER   B 1 94  ? -40.945 -0.037  20.414  1.00 48.02  ? 94  SER   B O    1 
ATOM   2532 C  CB   . SER   B 1 94  ? -38.681 2.188   20.001  1.00 48.75  ? 94  SER   B CB   1 
ATOM   2533 O  OG   . SER   B 1 94  ? -39.199 3.464   19.669  1.00 53.12  ? 94  SER   B OG   1 
ATOM   2534 N  N    . ALA   B 1 95  ? -41.813 2.010   20.862  1.00 44.30  ? 95  ALA   B N    1 
ATOM   2535 C  CA   . ALA   B 1 95  ? -43.126 1.781   20.223  1.00 45.32  ? 95  ALA   B CA   1 
ATOM   2536 C  C    . ALA   B 1 95  ? -43.792 3.118   19.871  1.00 41.34  ? 95  ALA   B C    1 
ATOM   2537 O  O    . ALA   B 1 95  ? -43.284 4.185   20.247  1.00 39.94  ? 95  ALA   B O    1 
ATOM   2538 C  CB   . ALA   B 1 95  ? -43.990 0.913   21.112  1.00 46.65  ? 95  ALA   B CB   1 
ATOM   2539 N  N    . SER   B 1 96  ? -44.877 3.061   19.114  1.00 41.24  ? 96  SER   B N    1 
ATOM   2540 C  CA   . SER   B 1 96  ? -45.592 4.265   18.649  1.00 46.30  ? 96  SER   B CA   1 
ATOM   2541 C  C    . SER   B 1 96  ? -47.027 3.916   18.296  1.00 45.36  ? 96  SER   B C    1 
ATOM   2542 O  O    . SER   B 1 96  ? -47.297 2.731   17.968  1.00 46.37  ? 96  SER   B O    1 
ATOM   2543 C  CB   . SER   B 1 96  ? -44.886 4.887   17.472  1.00 53.10  ? 96  SER   B CB   1 
ATOM   2544 O  OG   . SER   B 1 96  ? -44.795 3.956   16.393  1.00 54.67  ? 96  SER   B OG   1 
ATOM   2545 N  N    . THR   B 1 97  ? -47.884 4.939   18.354  1.00 48.52  ? 97  THR   B N    1 
ATOM   2546 C  CA   . THR   B 1 97  ? -49.279 4.962   17.837  1.00 46.72  ? 97  THR   B CA   1 
ATOM   2547 C  C    . THR   B 1 97  ? -49.370 6.168   16.899  1.00 46.06  ? 97  THR   B C    1 
ATOM   2548 O  O    . THR   B 1 97  ? -48.518 7.073   17.040  1.00 48.51  ? 97  THR   B O    1 
ATOM   2549 C  CB   . THR   B 1 97  ? -50.285 4.947   19.003  1.00 45.37  ? 97  THR   B CB   1 
ATOM   2550 O  OG1  . THR   B 1 97  ? -50.207 6.106   19.837  1.00 45.29  ? 97  THR   B OG1  1 
ATOM   2551 C  CG2  . THR   B 1 97  ? -50.067 3.751   19.893  1.00 46.91  ? 97  THR   B CG2  1 
ATOM   2552 N  N    . GLY   B 1 98  ? -50.332 6.171   15.971  1.00 49.96  ? 98  GLY   B N    1 
ATOM   2553 C  CA   . GLY   B 1 98  ? -50.565 7.287   15.022  1.00 54.37  ? 98  GLY   B CA   1 
ATOM   2554 C  C    . GLY   B 1 98  ? -52.031 7.698   15.011  1.00 55.85  ? 98  GLY   B C    1 
ATOM   2555 O  O    . GLY   B 1 98  ? -52.577 7.998   16.091  1.00 58.93  ? 98  GLY   B O    1 
ATOM   2556 N  N    . LEU   B 1 99  ? -52.674 7.708   13.842  1.00 54.09  ? 99  LEU   B N    1 
ATOM   2557 C  CA   . LEU   B 1 99  ? -54.154 7.822   13.768  1.00 50.66  ? 99  LEU   B CA   1 
ATOM   2558 C  C    . LEU   B 1 99  ? -54.765 6.603   14.466  1.00 49.91  ? 99  LEU   B C    1 
ATOM   2559 O  O    . LEU   B 1 99  ? -55.810 6.742   15.125  1.00 47.84  ? 99  LEU   B O    1 
ATOM   2560 C  CB   . LEU   B 1 99  ? -54.584 7.915   12.306  1.00 52.53  ? 99  LEU   B CB   1 
ATOM   2561 C  CG   . LEU   B 1 99  ? -56.084 7.743   12.044  1.00 55.87  ? 99  LEU   B CG   1 
ATOM   2562 C  CD1  . LEU   B 1 99  ? -56.902 8.824   12.738  1.00 53.00  ? 99  LEU   B CD1  1 
ATOM   2563 C  CD2  . LEU   B 1 99  ? -56.361 7.725   10.545  1.00 50.18  ? 99  LEU   B CD2  1 
ATOM   2564 N  N    . TYR   B 1 100 ? -54.102 5.449   14.339  1.00 58.63  ? 100 TYR   B N    1 
ATOM   2565 C  CA   . TYR   B 1 100 ? -54.484 4.163   14.984  1.00 55.47  ? 100 TYR   B CA   1 
ATOM   2566 C  C    . TYR   B 1 100 ? -53.540 3.867   16.156  1.00 46.37  ? 100 TYR   B C    1 
ATOM   2567 O  O    . TYR   B 1 100 ? -52.540 4.568   16.316  1.00 52.95  ? 100 TYR   B O    1 
ATOM   2568 C  CB   . TYR   B 1 100 ? -54.580 3.099   13.896  1.00 59.25  ? 100 TYR   B CB   1 
ATOM   2569 C  CG   . TYR   B 1 100 ? -55.714 3.351   12.930  1.00 62.94  ? 100 TYR   B CG   1 
ATOM   2570 C  CD1  . TYR   B 1 100 ? -57.022 3.406   13.387  1.00 62.09  ? 100 TYR   B CD1  1 
ATOM   2571 C  CD2  . TYR   B 1 100 ? -55.490 3.560   11.571  1.00 66.91  ? 100 TYR   B CD2  1 
ATOM   2572 C  CE1  . TYR   B 1 100 ? -58.082 3.625   12.523  1.00 68.86  ? 100 TYR   B CE1  1 
ATOM   2573 C  CE2  . TYR   B 1 100 ? -56.542 3.798   10.695  1.00 67.69  ? 100 TYR   B CE2  1 
ATOM   2574 C  CZ   . TYR   B 1 100 ? -57.843 3.811   11.175  1.00 68.72  ? 100 TYR   B CZ   1 
ATOM   2575 O  OH   . TYR   B 1 100 ? -58.910 4.018   10.358  1.00 74.66  ? 100 TYR   B OH   1 
ATOM   2576 N  N    . LYS   B 1 101 ? -53.925 2.936   17.021  1.00 48.67  ? 101 LYS   B N    1 
ATOM   2577 C  CA   . LYS   B 1 101 ? -53.386 2.790   18.403  1.00 54.90  ? 101 LYS   B CA   1 
ATOM   2578 C  C    . LYS   B 1 101 ? -53.515 1.342   18.901  1.00 51.33  ? 101 LYS   B C    1 
ATOM   2579 O  O    . LYS   B 1 101 ? -54.214 0.529   18.293  1.00 48.07  ? 101 LYS   B O    1 
ATOM   2580 C  CB   . LYS   B 1 101 ? -54.090 3.768   19.357  1.00 64.07  ? 101 LYS   B CB   1 
ATOM   2581 C  CG   . LYS   B 1 101 ? -55.614 3.812   19.269  1.00 66.52  ? 101 LYS   B CG   1 
ATOM   2582 C  CD   . LYS   B 1 101 ? -56.179 5.221   19.179  1.00 73.26  ? 101 LYS   B CD   1 
ATOM   2583 C  CE   . LYS   B 1 101 ? -57.661 5.311   19.501  1.00 81.54  ? 101 LYS   B CE   1 
ATOM   2584 N  NZ   . LYS   B 1 101 ? -58.215 6.668   19.236  1.00 77.01  ? 101 LYS   B NZ   1 
ATOM   2585 N  N    . GLU   B 1 102 ? -52.816 1.043   19.987  1.00 51.10  ? 102 GLU   B N    1 
ATOM   2586 C  CA   . GLU   B 1 102 ? -52.685 -0.303  20.601  1.00 48.11  ? 102 GLU   B CA   1 
ATOM   2587 C  C    . GLU   B 1 102 ? -51.887 -0.093  21.885  1.00 48.58  ? 102 GLU   B C    1 
ATOM   2588 O  O    . GLU   B 1 102 ? -51.058 0.859   21.912  1.00 53.77  ? 102 GLU   B O    1 
ATOM   2589 C  CB   . GLU   B 1 102 ? -51.929 -1.266  19.679  1.00 47.66  ? 102 GLU   B CB   1 
ATOM   2590 C  CG   . GLU   B 1 102 ? -50.441 -0.943  19.570  1.00 44.57  ? 102 GLU   B CG   1 
ATOM   2591 C  CD   . GLU   B 1 102 ? -49.698 -1.550  18.397  1.00 45.27  ? 102 GLU   B CD   1 
ATOM   2592 O  OE1  . GLU   B 1 102 ? -50.354 -2.037  17.454  1.00 44.54  ? 102 GLU   B OE1  1 
ATOM   2593 O  OE2  . GLU   B 1 102 ? -48.461 -1.513  18.424  1.00 43.17  ? 102 GLU   B OE2  1 
ATOM   2594 N  N    . THR   B 1 103 ? -52.109 -0.914  22.903  1.00 47.97  ? 103 THR   B N    1 
ATOM   2595 C  CA   . THR   B 1 103 ? -51.160 -1.028  24.041  1.00 54.16  ? 103 THR   B CA   1 
ATOM   2596 C  C    . THR   B 1 103 ? -49.847 -1.552  23.451  1.00 51.89  ? 103 THR   B C    1 
ATOM   2597 O  O    . THR   B 1 103 ? -49.930 -2.379  22.533  1.00 48.38  ? 103 THR   B O    1 
ATOM   2598 C  CB   . THR   B 1 103 ? -51.710 -1.923  25.159  1.00 57.07  ? 103 THR   B CB   1 
ATOM   2599 O  OG1  . THR   B 1 103 ? -51.847 -3.239  24.624  1.00 59.83  ? 103 THR   B OG1  1 
ATOM   2600 C  CG2  . THR   B 1 103 ? -53.038 -1.454  25.705  1.00 55.82  ? 103 THR   B CG2  1 
ATOM   2601 N  N    . ASN   B 1 104 ? -48.710 -1.005  23.888  1.00 55.11  ? 104 ASN   B N    1 
ATOM   2602 C  CA   . ASN   B 1 104 ? -47.345 -1.509  23.583  1.00 50.08  ? 104 ASN   B CA   1 
ATOM   2603 C  C    . ASN   B 1 104 ? -46.724 -1.970  24.913  1.00 47.00  ? 104 ASN   B C    1 
ATOM   2604 O  O    . ASN   B 1 104 ? -45.756 -1.393  25.362  1.00 44.88  ? 104 ASN   B O    1 
ATOM   2605 C  CB   . ASN   B 1 104 ? -46.573 -0.479  22.765  1.00 49.07  ? 104 ASN   B CB   1 
ATOM   2606 C  CG   . ASN   B 1 104 ? -47.214 -0.281  21.402  1.00 53.74  ? 104 ASN   B CG   1 
ATOM   2607 O  OD1  . ASN   B 1 104 ? -47.581 0.833   21.035  1.00 69.54  ? 104 ASN   B OD1  1 
ATOM   2608 N  ND2  . ASN   B 1 104 ? -47.379 -1.348  20.644  1.00 42.03  ? 104 ASN   B ND2  1 
ATOM   2609 N  N    . THR   B 1 105 ? -47.306 -3.005  25.510  1.00 44.28  ? 105 THR   B N    1 
ATOM   2610 C  CA   . THR   B 1 105 ? -46.979 -3.489  26.869  1.00 50.19  ? 105 THR   B CA   1 
ATOM   2611 C  C    . THR   B 1 105 ? -45.844 -4.521  26.802  1.00 49.44  ? 105 THR   B C    1 
ATOM   2612 O  O    . THR   B 1 105 ? -45.931 -5.459  25.991  1.00 53.94  ? 105 THR   B O    1 
ATOM   2613 C  CB   . THR   B 1 105 ? -48.223 -4.059  27.558  1.00 47.11  ? 105 THR   B CB   1 
ATOM   2614 O  OG1  . THR   B 1 105 ? -49.244 -3.076  27.406  1.00 45.94  ? 105 THR   B OG1  1 
ATOM   2615 C  CG2  . THR   B 1 105 ? -47.967 -4.349  29.016  1.00 44.00  ? 105 THR   B CG2  1 
ATOM   2616 N  N    . ILE   B 1 106 ? -44.809 -4.316  27.608  1.00 43.16  ? 106 ILE   B N    1 
ATOM   2617 C  CA   . ILE   B 1 106 ? -43.651 -5.235  27.734  1.00 52.01  ? 106 ILE   B CA   1 
ATOM   2618 C  C    . ILE   B 1 106 ? -43.713 -5.826  29.142  1.00 51.30  ? 106 ILE   B C    1 
ATOM   2619 O  O    . ILE   B 1 106 ? -43.723 -5.059  30.104  1.00 52.68  ? 106 ILE   B O    1 
ATOM   2620 C  CB   . ILE   B 1 106 ? -42.337 -4.487  27.463  1.00 57.56  ? 106 ILE   B CB   1 
ATOM   2621 C  CG1  . ILE   B 1 106 ? -42.305 -3.844  26.070  1.00 51.65  ? 106 ILE   B CG1  1 
ATOM   2622 C  CG2  . ILE   B 1 106 ? -41.164 -5.424  27.693  1.00 55.54  ? 106 ILE   B CG2  1 
ATOM   2623 C  CD1  . ILE   B 1 106 ? -42.280 -4.837  24.936  1.00 48.62  ? 106 ILE   B CD1  1 
ATOM   2624 N  N    . LEU   B 1 107 ? -43.832 -7.143  29.242  1.00 51.78  ? 107 LEU   B N    1 
ATOM   2625 C  CA   . LEU   B 1 107 ? -43.990 -7.856  30.534  1.00 53.85  ? 107 LEU   B CA   1 
ATOM   2626 C  C    . LEU   B 1 107 ? -42.629 -8.329  31.048  1.00 48.03  ? 107 LEU   B C    1 
ATOM   2627 O  O    . LEU   B 1 107 ? -42.521 -8.603  32.227  1.00 40.94  ? 107 LEU   B O    1 
ATOM   2628 C  CB   . LEU   B 1 107 ? -44.912 -9.054  30.331  1.00 54.31  ? 107 LEU   B CB   1 
ATOM   2629 C  CG   . LEU   B 1 107 ? -46.388 -8.725  30.141  1.00 60.75  ? 107 LEU   B CG   1 
ATOM   2630 C  CD1  . LEU   B 1 107 ? -46.655 -8.237  28.721  1.00 61.64  ? 107 LEU   B CD1  1 
ATOM   2631 C  CD2  . LEU   B 1 107 ? -47.235 -9.954  30.458  1.00 61.69  ? 107 LEU   B CD2  1 
ATOM   2632 N  N    . SER   B 1 108 ? -41.653 -8.485  30.162  1.00 48.94  ? 108 SER   B N    1 
ATOM   2633 C  CA   . SER   B 1 108 ? -40.303 -8.988  30.495  1.00 46.28  ? 108 SER   B CA   1 
ATOM   2634 C  C    . SER   B 1 108 ? -39.344 -8.686  29.350  1.00 44.83  ? 108 SER   B C    1 
ATOM   2635 O  O    . SER   B 1 108 ? -39.759 -8.722  28.201  1.00 42.51  ? 108 SER   B O    1 
ATOM   2636 C  CB   . SER   B 1 108 ? -40.323 -10.457 30.790  1.00 43.27  ? 108 SER   B CB   1 
ATOM   2637 O  OG   . SER   B 1 108 ? -40.432 -11.209 29.592  1.00 42.03  ? 108 SER   B OG   1 
ATOM   2638 N  N    . TRP   B 1 109 ? -38.075 -8.529  29.687  1.00 44.85  ? 109 TRP   B N    1 
ATOM   2639 C  CA   . TRP   B 1 109 ? -36.998 -8.232  28.731  1.00 43.86  ? 109 TRP   B CA   1 
ATOM   2640 C  C    . TRP   B 1 109 ? -35.722 -8.754  29.361  1.00 42.45  ? 109 TRP   B C    1 
ATOM   2641 O  O    . TRP   B 1 109 ? -35.517 -8.487  30.547  1.00 41.43  ? 109 TRP   B O    1 
ATOM   2642 C  CB   . TRP   B 1 109 ? -36.943 -6.714  28.478  1.00 44.68  ? 109 TRP   B CB   1 
ATOM   2643 C  CG   . TRP   B 1 109 ? -35.876 -6.250  27.535  1.00 39.72  ? 109 TRP   B CG   1 
ATOM   2644 C  CD1  . TRP   B 1 109 ? -35.300 -6.953  26.519  1.00 39.92  ? 109 TRP   B CD1  1 
ATOM   2645 C  CD2  . TRP   B 1 109 ? -35.244 -4.960  27.541  1.00 41.32  ? 109 TRP   B CD2  1 
ATOM   2646 N  NE1  . TRP   B 1 109 ? -34.361 -6.184  25.877  1.00 45.38  ? 109 TRP   B NE1  1 
ATOM   2647 C  CE2  . TRP   B 1 109 ? -34.313 -4.953  26.482  1.00 43.36  ? 109 TRP   B CE2  1 
ATOM   2648 C  CE3  . TRP   B 1 109 ? -35.411 -3.803  28.310  1.00 43.72  ? 109 TRP   B CE3  1 
ATOM   2649 C  CZ2  . TRP   B 1 109 ? -33.533 -3.840  26.192  1.00 46.36  ? 109 TRP   B CZ2  1 
ATOM   2650 C  CZ3  . TRP   B 1 109 ? -34.657 -2.692  28.011  1.00 44.01  ? 109 TRP   B CZ3  1 
ATOM   2651 C  CH2  . TRP   B 1 109 ? -33.723 -2.720  26.972  1.00 48.92  ? 109 TRP   B CH2  1 
ATOM   2652 N  N    . SER   B 1 110 ? -34.926 -9.450  28.570  1.00 42.15  ? 110 SER   B N    1 
ATOM   2653 C  CA   . SER   B 1 110 ? -33.575 -9.929  28.929  1.00 47.70  ? 110 SER   B CA   1 
ATOM   2654 C  C    . SER   B 1 110 ? -32.653 -9.712  27.730  1.00 44.81  ? 110 SER   B C    1 
ATOM   2655 O  O    . SER   B 1 110 ? -33.173 -9.582  26.611  1.00 42.22  ? 110 SER   B O    1 
ATOM   2656 C  CB   . SER   B 1 110 ? -33.590 -11.363 29.321  1.00 43.61  ? 110 SER   B CB   1 
ATOM   2657 O  OG   . SER   B 1 110 ? -33.594 -12.147 28.155  1.00 47.15  ? 110 SER   B OG   1 
ATOM   2658 N  N    . PHE   B 1 111 ? -31.349 -9.659  27.996  1.00 42.25  ? 111 PHE   B N    1 
ATOM   2659 C  CA   . PHE   B 1 111 ? -30.290 -9.311  27.023  1.00 40.86  ? 111 PHE   B CA   1 
ATOM   2660 C  C    . PHE   B 1 111 ? -28.965 -9.861  27.521  1.00 39.19  ? 111 PHE   B C    1 
ATOM   2661 O  O    . PHE   B 1 111 ? -28.728 -9.814  28.735  1.00 44.00  ? 111 PHE   B O    1 
ATOM   2662 C  CB   . PHE   B 1 111 ? -30.161 -7.801  26.875  1.00 41.45  ? 111 PHE   B CB   1 
ATOM   2663 C  CG   . PHE   B 1 111 ? -29.030 -7.367  25.983  1.00 40.94  ? 111 PHE   B CG   1 
ATOM   2664 C  CD1  . PHE   B 1 111 ? -29.190 -7.331  24.605  1.00 37.45  ? 111 PHE   B CD1  1 
ATOM   2665 C  CD2  . PHE   B 1 111 ? -27.808 -6.979  26.527  1.00 40.12  ? 111 PHE   B CD2  1 
ATOM   2666 C  CE1  . PHE   B 1 111 ? -28.145 -6.926  23.783  1.00 40.80  ? 111 PHE   B CE1  1 
ATOM   2667 C  CE2  . PHE   B 1 111 ? -26.779 -6.552  25.695  1.00 40.64  ? 111 PHE   B CE2  1 
ATOM   2668 C  CZ   . PHE   B 1 111 ? -26.941 -6.543  24.326  1.00 37.68  ? 111 PHE   B CZ   1 
ATOM   2669 N  N    . THR   B 1 112 ? -28.166 -10.380 26.604  1.00 38.53  ? 112 THR   B N    1 
ATOM   2670 C  CA   . THR   B 1 112 ? -26.849 -10.986 26.885  1.00 44.23  ? 112 THR   B CA   1 
ATOM   2671 C  C    . THR   B 1 112 ? -25.906 -10.536 25.776  1.00 42.05  ? 112 THR   B C    1 
ATOM   2672 O  O    . THR   B 1 112 ? -26.291 -10.655 24.640  1.00 49.26  ? 112 THR   B O    1 
ATOM   2673 C  CB   . THR   B 1 112 ? -26.933 -12.519 26.984  1.00 48.08  ? 112 THR   B CB   1 
ATOM   2674 O  OG1  . THR   B 1 112 ? -27.704 -12.943 28.108  1.00 56.44  ? 112 THR   B OG1  1 
ATOM   2675 C  CG2  . THR   B 1 112 ? -25.583 -13.166 27.166  1.00 54.78  ? 112 THR   B CG2  1 
ATOM   2676 N  N    . SER   B 1 113 ? -24.721 -10.043 26.121  1.00 45.60  ? 113 SER   B N    1 
ATOM   2677 C  CA   . SER   B 1 113 ? -23.639 -9.673  25.182  1.00 47.07  ? 113 SER   B CA   1 
ATOM   2678 C  C    . SER   B 1 113 ? -22.320 -10.293 25.657  1.00 45.11  ? 113 SER   B C    1 
ATOM   2679 O  O    . SER   B 1 113 ? -22.052 -10.157 26.843  1.00 46.91  ? 113 SER   B O    1 
ATOM   2680 C  CB   . SER   B 1 113 ? -23.551 -8.181  25.104  1.00 48.60  ? 113 SER   B CB   1 
ATOM   2681 O  OG   . SER   B 1 113 ? -22.557 -7.820  24.165  1.00 62.68  ? 113 SER   B OG   1 
ATOM   2682 N  N    . LYS   B 1 114 ? -21.552 -10.935 24.774  1.00 40.86  ? 114 LYS   B N    1 
ATOM   2683 C  CA   . LYS   B 1 114 ? -20.214 -11.508 25.067  1.00 50.18  ? 114 LYS   B CA   1 
ATOM   2684 C  C    . LYS   B 1 114 ? -19.235 -11.082 23.986  1.00 54.21  ? 114 LYS   B C    1 
ATOM   2685 O  O    . LYS   B 1 114 ? -19.650 -11.087 22.836  1.00 54.92  ? 114 LYS   B O    1 
ATOM   2686 C  CB   . LYS   B 1 114 ? -20.225 -13.038 25.086  1.00 53.27  ? 114 LYS   B CB   1 
ATOM   2687 C  CG   . LYS   B 1 114 ? -21.215 -13.614 26.081  1.00 64.11  ? 114 LYS   B CG   1 
ATOM   2688 C  CD   . LYS   B 1 114 ? -21.086 -15.078 26.379  1.00 70.43  ? 114 LYS   B CD   1 
ATOM   2689 C  CE   . LYS   B 1 114 ? -21.893 -15.455 27.611  1.00 76.78  ? 114 LYS   B CE   1 
ATOM   2690 N  NZ   . LYS   B 1 114 ? -21.813 -16.904 27.912  1.00 85.66  ? 114 LYS   B NZ   1 
ATOM   2691 N  N    . LEU   B 1 115 ? -18.010 -10.716 24.382  1.00 60.12  ? 115 LEU   B N    1 
ATOM   2692 C  CA   . LEU   B 1 115 ? -16.792 -10.660 23.528  1.00 57.76  ? 115 LEU   B CA   1 
ATOM   2693 C  C    . LEU   B 1 115 ? -15.772 -11.664 24.065  1.00 60.62  ? 115 LEU   B C    1 
ATOM   2694 O  O    . LEU   B 1 115 ? -15.210 -11.410 25.123  1.00 70.96  ? 115 LEU   B O    1 
ATOM   2695 C  CB   . LEU   B 1 115 ? -16.207 -9.252  23.576  1.00 53.56  ? 115 LEU   B CB   1 
ATOM   2696 C  CG   . LEU   B 1 115 ? -17.211 -8.142  23.321  1.00 48.97  ? 115 LEU   B CG   1 
ATOM   2697 C  CD1  . LEU   B 1 115 ? -16.601 -6.787  23.615  1.00 49.33  ? 115 LEU   B CD1  1 
ATOM   2698 C  CD2  . LEU   B 1 115 ? -17.712 -8.175  21.897  1.00 57.41  ? 115 LEU   B CD2  1 
ATOM   2699 N  N    . LYS   B 1 116 ? -15.592 -12.781 23.367  1.00 70.51  ? 116 LYS   B N    1 
ATOM   2700 C  CA   . LYS   B 1 116 ? -14.562 -13.812 23.638  1.00 67.49  ? 116 LYS   B CA   1 
ATOM   2701 C  C    . LYS   B 1 116 ? -13.391 -13.508 22.720  1.00 69.35  ? 116 LYS   B C    1 
ATOM   2702 O  O    . LYS   B 1 116 ? -13.615 -12.884 21.692  1.00 74.01  ? 116 LYS   B O    1 
ATOM   2703 C  CB   . LYS   B 1 116 ? -15.115 -15.224 23.405  1.00 70.63  ? 116 LYS   B CB   1 
ATOM   2704 C  CG   . LYS   B 1 116 ? -16.515 -15.465 23.968  1.00 74.09  ? 116 LYS   B CG   1 
ATOM   2705 C  CD   . LYS   B 1 116 ? -17.094 -16.867 23.791  1.00 75.87  ? 116 LYS   B CD   1 
ATOM   2706 C  CE   . LYS   B 1 116 ? -18.525 -16.917 24.298  1.00 77.81  ? 116 LYS   B CE   1 
ATOM   2707 N  NZ   . LYS   B 1 116 ? -19.021 -18.291 24.524  1.00 74.90  ? 116 LYS   B NZ   1 
ATOM   2708 N  N    . SER   B 1 117 ? -12.177 -13.816 23.145  1.00 94.04  ? 117 SER   B N    1 
ATOM   2709 C  CA   . SER   B 1 117 ? -11.006 -13.482 22.306  1.00 92.35  ? 117 SER   B CA   1 
ATOM   2710 C  C    . SER   B 1 117 ? -9.919  -14.511 22.557  1.00 99.65  ? 117 SER   B C    1 
ATOM   2711 O  O    . SER   B 1 117 ? -10.249 -15.638 22.964  1.00 79.61  ? 117 SER   B O    1 
ATOM   2712 C  CB   . SER   B 1 117 ? -10.501 -12.113 22.635  1.00 95.49  ? 117 SER   B CB   1 
ATOM   2713 O  OG   . SER   B 1 117 ? -9.454  -11.740 21.757  1.00 103.27 ? 117 SER   B OG   1 
ATOM   2714 N  N    . ASN   B 1 118 ? -8.678  -14.132 22.271  1.00 113.20 ? 118 ASN   B N    1 
ATOM   2715 C  CA   . ASN   B 1 118 ? -7.565  -15.069 22.541  1.00 118.49 ? 118 ASN   B CA   1 
ATOM   2716 C  C    . ASN   B 1 118 ? -6.434  -14.405 23.316  1.00 123.12 ? 118 ASN   B C    1 
ATOM   2717 O  O    . ASN   B 1 118 ? -5.289  -14.746 23.036  1.00 139.59 ? 118 ASN   B O    1 
ATOM   2718 C  CB   . ASN   B 1 118 ? -7.147  -15.908 21.340  1.00 111.51 ? 118 ASN   B CB   1 
ATOM   2719 C  CG   . ASN   B 1 118 ? -7.440  -17.359 21.634  1.00 115.75 ? 118 ASN   B CG   1 
ATOM   2720 O  OD1  . ASN   B 1 118 ? -6.854  -18.255 21.049  1.00 111.53 ? 118 ASN   B OD1  1 
ATOM   2721 N  ND2  . ASN   B 1 118 ? -8.337  -17.592 22.578  1.00 113.16 ? 118 ASN   B ND2  1 
ATOM   2722 N  N    . SER   B 1 119 ? -6.733  -13.502 24.250  1.00 129.41 ? 119 SER   B N    1 
ATOM   2723 C  CA   . SER   B 1 119 ? -5.608  -12.934 25.036  1.00 139.76 ? 119 SER   B CA   1 
ATOM   2724 C  C    . SER   B 1 119 ? -4.960  -14.088 25.819  1.00 158.92 ? 119 SER   B C    1 
ATOM   2725 O  O    . SER   B 1 119 ? -3.716  -14.203 25.772  1.00 150.30 ? 119 SER   B O    1 
ATOM   2726 C  CB   . SER   B 1 119 ? -6.064  -11.799 25.911  1.00 122.77 ? 119 SER   B CB   1 
ATOM   2727 O  OG   . SER   B 1 119 ? -6.384  -10.660 25.121  1.00 103.54 ? 119 SER   B OG   1 
ATOM   2728 N  N    . THR   B 1 120 ? -5.796  -14.934 26.442  1.00 165.36 ? 120 THR   B N    1 
ATOM   2729 C  CA   . THR   B 1 120 ? -5.425  -16.192 27.151  1.00 152.50 ? 120 THR   B CA   1 
ATOM   2730 C  C    . THR   B 1 120 ? -6.670  -17.086 27.174  1.00 153.35 ? 120 THR   B C    1 
ATOM   2731 O  O    . THR   B 1 120 ? -6.978  -17.679 26.126  1.00 128.89 ? 120 THR   B O    1 
ATOM   2732 C  CB   . THR   B 1 120 ? -5.007  -15.976 28.610  1.00 145.57 ? 120 THR   B CB   1 
ATOM   2733 O  OG1  . THR   B 1 120 ? -6.005  -15.201 29.275  1.00 145.17 ? 120 THR   B OG1  1 
ATOM   2734 C  CG2  . THR   B 1 120 ? -3.632  -15.366 28.768  1.00 128.23 ? 120 THR   B CG2  1 
ATOM   2735 N  N    . HIS   B 1 121 ? -7.337  -17.185 28.333  1.00 165.37 ? 121 HIS   B N    1 
ATOM   2736 C  CA   . HIS   B 1 121 ? -8.589  -17.985 28.469  1.00 158.30 ? 121 HIS   B CA   1 
ATOM   2737 C  C    . HIS   B 1 121 ? -9.767  -17.131 28.958  1.00 139.62 ? 121 HIS   B C    1 
ATOM   2738 O  O    . HIS   B 1 121 ? -10.776 -17.739 29.350  1.00 119.02 ? 121 HIS   B O    1 
ATOM   2739 C  CB   . HIS   B 1 121 ? -8.436  -19.237 29.360  1.00 154.30 ? 121 HIS   B CB   1 
ATOM   2740 C  CG   . HIS   B 1 121 ? -7.196  -19.366 30.186  1.00 160.42 ? 121 HIS   B CG   1 
ATOM   2741 N  ND1  . HIS   B 1 121 ? -5.977  -18.826 29.822  1.00 163.69 ? 121 HIS   B ND1  1 
ATOM   2742 C  CD2  . HIS   B 1 121 ? -6.977  -20.021 31.347  1.00 149.51 ? 121 HIS   B CD2  1 
ATOM   2743 C  CE1  . HIS   B 1 121 ? -5.072  -19.118 30.734  1.00 140.54 ? 121 HIS   B CE1  1 
ATOM   2744 N  NE2  . HIS   B 1 121 ? -5.660  -19.855 31.680  1.00 141.21 ? 121 HIS   B NE2  1 
ATOM   2745 N  N    . GLU   B 1 122 ? -9.663  -15.797 28.908  1.00 132.38 ? 122 GLU   B N    1 
ATOM   2746 C  CA   . GLU   B 1 122 ? -10.732 -14.920 29.465  1.00 119.02 ? 122 GLU   B CA   1 
ATOM   2747 C  C    . GLU   B 1 122 ? -11.459 -14.100 28.381  1.00 111.38 ? 122 GLU   B C    1 
ATOM   2748 O  O    . GLU   B 1 122 ? -10.821 -13.690 27.403  1.00 91.74  ? 122 GLU   B O    1 
ATOM   2749 C  CB   . GLU   B 1 122 ? -10.178 -14.132 30.656  1.00 123.14 ? 122 GLU   B CB   1 
ATOM   2750 C  CG   . GLU   B 1 122 ? -9.571  -15.021 31.736  1.00 123.30 ? 122 GLU   B CG   1 
ATOM   2751 C  CD   . GLU   B 1 122 ? -9.003  -14.305 32.955  1.00 123.32 ? 122 GLU   B CD   1 
ATOM   2752 O  OE1  . GLU   B 1 122 ? -8.208  -13.361 32.762  1.00 122.40 ? 122 GLU   B OE1  1 
ATOM   2753 O  OE2  . GLU   B 1 122 ? -9.350  -14.694 34.099  1.00 107.20 ? 122 GLU   B OE2  1 
ATOM   2754 N  N    . THR   B 1 123 ? -12.745 -13.833 28.642  1.00 100.85 ? 123 THR   B N    1 
ATOM   2755 C  CA   . THR   B 1 123 ? -13.811 -13.196 27.800  1.00 86.24  ? 123 THR   B CA   1 
ATOM   2756 C  C    . THR   B 1 123 ? -14.495 -12.041 28.561  1.00 74.48  ? 123 THR   B C    1 
ATOM   2757 O  O    . THR   B 1 123 ? -14.390 -12.047 29.791  1.00 82.54  ? 123 THR   B O    1 
ATOM   2758 C  CB   . THR   B 1 123 ? -14.824 -14.281 27.371  1.00 97.90  ? 123 THR   B CB   1 
ATOM   2759 O  OG1  . THR   B 1 123 ? -15.796 -14.570 28.378  1.00 77.75  ? 123 THR   B OG1  1 
ATOM   2760 C  CG2  . THR   B 1 123 ? -14.178 -15.611 27.022  1.00 98.02  ? 123 THR   B CG2  1 
ATOM   2761 N  N    . ASN   B 1 124 ? -15.208 -11.119 27.882  1.00 65.55  ? 124 ASN   B N    1 
ATOM   2762 C  CA   . ASN   B 1 124 ? -16.002 -10.000 28.490  1.00 61.17  ? 124 ASN   B CA   1 
ATOM   2763 C  C    . ASN   B 1 124 ? -17.514 -10.125 28.231  1.00 61.01  ? 124 ASN   B C    1 
ATOM   2764 O  O    . ASN   B 1 124 ? -17.884 -10.387 27.072  1.00 69.12  ? 124 ASN   B O    1 
ATOM   2765 C  CB   . ASN   B 1 124 ? -15.608 -8.636  27.930  1.00 63.47  ? 124 ASN   B CB   1 
ATOM   2766 C  CG   . ASN   B 1 124 ? -14.332 -8.108  28.534  1.00 71.80  ? 124 ASN   B CG   1 
ATOM   2767 O  OD1  . ASN   B 1 124 ? -13.684 -8.791  29.328  1.00 77.84  ? 124 ASN   B OD1  1 
ATOM   2768 N  ND2  . ASN   B 1 124 ? -13.977 -6.887  28.173  1.00 73.43  ? 124 ASN   B ND2  1 
ATOM   2769 N  N    . ALA   B 1 125 ? -18.366 -9.829  29.228  1.00 52.32  ? 125 ALA   B N    1 
ATOM   2770 C  CA   . ALA   B 1 125 ? -19.818 -10.124 29.190  1.00 43.74  ? 125 ALA   B CA   1 
ATOM   2771 C  C    . ALA   B 1 125 ? -20.664 -9.114  29.956  1.00 46.82  ? 125 ALA   B C    1 
ATOM   2772 O  O    . ALA   B 1 125 ? -20.247 -8.657  31.045  1.00 47.55  ? 125 ALA   B O    1 
ATOM   2773 C  CB   . ALA   B 1 125 ? -20.105 -11.477 29.770  1.00 47.31  ? 125 ALA   B CB   1 
ATOM   2774 N  N    . LEU   B 1 126 ? -21.892 -8.926  29.460  1.00 43.36  ? 126 LEU   B N    1 
ATOM   2775 C  CA   . LEU   B 1 126 ? -22.997 -8.275  30.188  1.00 42.35  ? 126 LEU   B CA   1 
ATOM   2776 C  C    . LEU   B 1 126 ? -24.285 -9.081  30.005  1.00 41.59  ? 126 LEU   B C    1 
ATOM   2777 O  O    . LEU   B 1 126 ? -24.491 -9.630  28.931  1.00 44.98  ? 126 LEU   B O    1 
ATOM   2778 C  CB   . LEU   B 1 126 ? -23.144 -6.858  29.632  1.00 42.90  ? 126 LEU   B CB   1 
ATOM   2779 C  CG   . LEU   B 1 126 ? -24.356 -6.088  30.143  1.00 43.24  ? 126 LEU   B CG   1 
ATOM   2780 C  CD1  . LEU   B 1 126 ? -24.078 -5.481  31.505  1.00 44.69  ? 126 LEU   B CD1  1 
ATOM   2781 C  CD2  . LEU   B 1 126 ? -24.768 -5.024  29.144  1.00 47.86  ? 126 LEU   B CD2  1 
ATOM   2782 N  N    . HIS   B 1 127 ? -25.143 -9.095  31.015  1.00 41.88  ? 127 HIS   B N    1 
ATOM   2783 C  CA   . HIS   B 1 127 ? -26.452 -9.789  31.006  1.00 41.48  ? 127 HIS   B CA   1 
ATOM   2784 C  C    . HIS   B 1 127 ? -27.390 -9.069  31.954  1.00 40.47  ? 127 HIS   B C    1 
ATOM   2785 O  O    . HIS   B 1 127 ? -27.000 -8.929  33.113  1.00 41.63  ? 127 HIS   B O    1 
ATOM   2786 C  CB   . HIS   B 1 127 ? -26.312 -11.266 31.435  1.00 47.99  ? 127 HIS   B CB   1 
ATOM   2787 C  CG   . HIS   B 1 127 ? -27.609 -12.009 31.617  1.00 47.55  ? 127 HIS   B CG   1 
ATOM   2788 N  ND1  . HIS   B 1 127 ? -28.459 -12.337 30.544  1.00 41.66  ? 127 HIS   B ND1  1 
ATOM   2789 C  CD2  . HIS   B 1 127 ? -28.211 -12.488 32.732  1.00 45.00  ? 127 HIS   B CD2  1 
ATOM   2790 C  CE1  . HIS   B 1 127 ? -29.508 -12.998 31.011  1.00 47.00  ? 127 HIS   B CE1  1 
ATOM   2791 N  NE2  . HIS   B 1 127 ? -29.387 -13.113 32.345  1.00 44.47  ? 127 HIS   B NE2  1 
ATOM   2792 N  N    . PHE   B 1 128 ? -28.564 -8.630  31.483  1.00 42.17  ? 128 PHE   B N    1 
ATOM   2793 C  CA   . PHE   B 1 128 ? -29.660 -8.212  32.391  1.00 42.60  ? 128 PHE   B CA   1 
ATOM   2794 C  C    . PHE   B 1 128 ? -30.930 -8.978  32.029  1.00 48.45  ? 128 PHE   B C    1 
ATOM   2795 O  O    . PHE   B 1 128 ? -31.049 -9.490  30.876  1.00 39.48  ? 128 PHE   B O    1 
ATOM   2796 C  CB   . PHE   B 1 128 ? -29.867 -6.700  32.363  1.00 47.37  ? 128 PHE   B CB   1 
ATOM   2797 C  CG   . PHE   B 1 128 ? -30.125 -6.103  31.003  1.00 52.07  ? 128 PHE   B CG   1 
ATOM   2798 C  CD1  . PHE   B 1 128 ? -31.415 -6.020  30.501  1.00 49.47  ? 128 PHE   B CD1  1 
ATOM   2799 C  CD2  . PHE   B 1 128 ? -29.084 -5.608  30.233  1.00 49.29  ? 128 PHE   B CD2  1 
ATOM   2800 C  CE1  . PHE   B 1 128 ? -31.663 -5.454  29.260  1.00 44.70  ? 128 PHE   B CE1  1 
ATOM   2801 C  CE2  . PHE   B 1 128 ? -29.336 -5.062  28.988  1.00 46.73  ? 128 PHE   B CE2  1 
ATOM   2802 C  CZ   . PHE   B 1 128 ? -30.623 -4.977  28.513  1.00 45.20  ? 128 PHE   B CZ   1 
ATOM   2803 N  N    . MET   B 1 129 ? -31.821 -9.079  33.019  1.00 43.39  ? 129 MET   B N    1 
ATOM   2804 C  CA   . MET   B 1 129 ? -33.130 -9.737  32.912  1.00 43.15  ? 129 MET   B CA   1 
ATOM   2805 C  C    . MET   B 1 129 ? -34.095 -8.929  33.749  1.00 43.10  ? 129 MET   B C    1 
ATOM   2806 O  O    . MET   B 1 129 ? -33.830 -8.799  34.928  1.00 46.65  ? 129 MET   B O    1 
ATOM   2807 C  CB   . MET   B 1 129 ? -33.112 -11.159 33.465  1.00 50.96  ? 129 MET   B CB   1 
ATOM   2808 C  CG   . MET   B 1 129 ? -34.412 -11.923 33.191  1.00 61.65  ? 129 MET   B CG   1 
ATOM   2809 S  SD   . MET   B 1 129 ? -34.355 -13.686 33.689  1.00 80.98  ? 129 MET   B SD   1 
ATOM   2810 C  CE   . MET   B 1 129 ? -32.739 -14.241 33.127  1.00 77.26  ? 129 MET   B CE   1 
ATOM   2811 N  N    . PHE   B 1 130 ? -35.144 -8.390  33.139  1.00 45.41  ? 130 PHE   B N    1 
ATOM   2812 C  CA   . PHE   B 1 130 ? -36.294 -7.794  33.857  1.00 49.19  ? 130 PHE   B CA   1 
ATOM   2813 C  C    . PHE   B 1 130 ? -37.483 -8.710  33.608  1.00 48.32  ? 130 PHE   B C    1 
ATOM   2814 O  O    . PHE   B 1 130 ? -37.849 -8.849  32.447  1.00 46.41  ? 130 PHE   B O    1 
ATOM   2815 C  CB   . PHE   B 1 130 ? -36.612 -6.370  33.383  1.00 52.12  ? 130 PHE   B CB   1 
ATOM   2816 C  CG   . PHE   B 1 130 ? -35.449 -5.411  33.341  1.00 52.54  ? 130 PHE   B CG   1 
ATOM   2817 C  CD1  . PHE   B 1 130 ? -35.063 -4.720  34.473  1.00 55.29  ? 130 PHE   B CD1  1 
ATOM   2818 C  CD2  . PHE   B 1 130 ? -34.770 -5.168  32.155  1.00 57.60  ? 130 PHE   B CD2  1 
ATOM   2819 C  CE1  . PHE   B 1 130 ? -34.005 -3.830  34.429  1.00 60.26  ? 130 PHE   B CE1  1 
ATOM   2820 C  CE2  . PHE   B 1 130 ? -33.726 -4.257  32.107  1.00 56.47  ? 130 PHE   B CE2  1 
ATOM   2821 C  CZ   . PHE   B 1 130 ? -33.327 -3.612  33.252  1.00 60.82  ? 130 PHE   B CZ   1 
ATOM   2822 N  N    . ASN   B 1 131 ? -38.016 -9.311  34.671  1.00 50.20  ? 131 ASN   B N    1 
ATOM   2823 C  CA   . ASN   B 1 131 ? -39.255 -10.124 34.658  1.00 52.09  ? 131 ASN   B CA   1 
ATOM   2824 C  C    . ASN   B 1 131 ? -40.370 -9.310  35.325  1.00 52.46  ? 131 ASN   B C    1 
ATOM   2825 O  O    . ASN   B 1 131 ? -41.520 -9.718  35.241  1.00 55.25  ? 131 ASN   B O    1 
ATOM   2826 C  CB   . ASN   B 1 131 ? -39.048 -11.496 35.316  1.00 54.15  ? 131 ASN   B CB   1 
ATOM   2827 C  CG   . ASN   B 1 131 ? -38.492 -12.539 34.365  1.00 63.57  ? 131 ASN   B CG   1 
ATOM   2828 O  OD1  . ASN   B 1 131 ? -39.009 -12.724 33.267  1.00 72.60  ? 131 ASN   B OD1  1 
ATOM   2829 N  ND2  . ASN   B 1 131 ? -37.442 -13.237 34.765  1.00 68.56  ? 131 ASN   B ND2  1 
ATOM   2830 N  N    . GLN   B 1 132 ? -40.036 -8.226  36.011  1.00 55.51  ? 132 GLN   B N    1 
ATOM   2831 C  CA   . GLN   B 1 132 ? -41.014 -7.189  36.410  1.00 68.39  ? 132 GLN   B CA   1 
ATOM   2832 C  C    . GLN   B 1 132 ? -40.273 -5.845  36.468  1.00 65.81  ? 132 GLN   B C    1 
ATOM   2833 O  O    . GLN   B 1 132 ? -39.097 -5.831  36.846  1.00 70.35  ? 132 GLN   B O    1 
ATOM   2834 C  CB   . GLN   B 1 132 ? -41.680 -7.588  37.729  1.00 79.22  ? 132 GLN   B CB   1 
ATOM   2835 C  CG   . GLN   B 1 132 ? -40.754 -7.495  38.941  1.00 86.41  ? 132 GLN   B CG   1 
ATOM   2836 C  CD   . GLN   B 1 132 ? -41.194 -8.303  40.146  1.00 98.95  ? 132 GLN   B CD   1 
ATOM   2837 O  OE1  . GLN   B 1 132 ? -42.293 -8.870  40.211  1.00 88.74  ? 132 GLN   B OE1  1 
ATOM   2838 N  NE2  . GLN   B 1 132 ? -40.308 -8.370  41.127  1.00 94.99  ? 132 GLN   B NE2  1 
ATOM   2839 N  N    . PHE   B 1 133 ? -40.940 -4.761  36.090  1.00 57.79  ? 133 PHE   B N    1 
ATOM   2840 C  CA   . PHE   B 1 133 ? -40.436 -3.375  36.225  1.00 53.46  ? 133 PHE   B CA   1 
ATOM   2841 C  C    . PHE   B 1 133 ? -41.147 -2.714  37.414  1.00 60.90  ? 133 PHE   B C    1 
ATOM   2842 O  O    . PHE   B 1 133 ? -42.312 -3.035  37.694  1.00 55.44  ? 133 PHE   B O    1 
ATOM   2843 C  CB   . PHE   B 1 133 ? -40.694 -2.598  34.934  1.00 50.93  ? 133 PHE   B CB   1 
ATOM   2844 C  CG   . PHE   B 1 133 ? -40.290 -3.339  33.691  1.00 44.42  ? 133 PHE   B CG   1 
ATOM   2845 C  CD1  . PHE   B 1 133 ? -41.102 -4.322  33.154  1.00 45.88  ? 133 PHE   B CD1  1 
ATOM   2846 C  CD2  . PHE   B 1 133 ? -39.090 -3.070  33.074  1.00 42.35  ? 133 PHE   B CD2  1 
ATOM   2847 C  CE1  . PHE   B 1 133 ? -40.719 -5.014  32.020  1.00 44.81  ? 133 PHE   B CE1  1 
ATOM   2848 C  CE2  . PHE   B 1 133 ? -38.704 -3.770  31.946  1.00 42.56  ? 133 PHE   B CE2  1 
ATOM   2849 C  CZ   . PHE   B 1 133 ? -39.524 -4.738  31.416  1.00 42.73  ? 133 PHE   B CZ   1 
ATOM   2850 N  N    . SER   B 1 134 ? -40.462 -1.804  38.102  1.00 64.97  ? 134 SER   B N    1 
ATOM   2851 C  CA   . SER   B 1 134 ? -41.003 -1.036  39.252  1.00 69.69  ? 134 SER   B CA   1 
ATOM   2852 C  C    . SER   B 1 134 ? -41.144 0.440   38.863  1.00 69.16  ? 134 SER   B C    1 
ATOM   2853 O  O    . SER   B 1 134 ? -40.626 0.809   37.783  1.00 60.32  ? 134 SER   B O    1 
ATOM   2854 C  CB   . SER   B 1 134 ? -40.135 -1.225  40.473  1.00 75.55  ? 134 SER   B CB   1 
ATOM   2855 O  OG   . SER   B 1 134 ? -38.753 -1.111  40.155  1.00 81.58  ? 134 SER   B OG   1 
ATOM   2856 N  N    . LYS   B 1 135 ? -41.796 1.227   39.732  1.00 80.57  ? 135 LYS   B N    1 
ATOM   2857 C  CA   . LYS   B 1 135 ? -42.171 2.659   39.534  1.00 89.24  ? 135 LYS   B CA   1 
ATOM   2858 C  C    . LYS   B 1 135 ? -40.904 3.505   39.334  1.00 81.33  ? 135 LYS   B C    1 
ATOM   2859 O  O    . LYS   B 1 135 ? -40.964 4.486   38.550  1.00 81.62  ? 135 LYS   B O    1 
ATOM   2860 C  CB   . LYS   B 1 135 ? -42.971 3.223   40.719  1.00 92.89  ? 135 LYS   B CB   1 
ATOM   2861 C  CG   . LYS   B 1 135 ? -44.185 2.414   41.169  1.00 111.77 ? 135 LYS   B CG   1 
ATOM   2862 C  CD   . LYS   B 1 135 ? -45.520 2.831   40.564  1.00 116.14 ? 135 LYS   B CD   1 
ATOM   2863 C  CE   . LYS   B 1 135 ? -46.649 1.902   40.974  1.00 113.43 ? 135 LYS   B CE   1 
ATOM   2864 N  NZ   . LYS   B 1 135 ? -47.960 2.343   40.447  1.00 113.40 ? 135 LYS   B NZ   1 
ATOM   2865 N  N    . ASP   B 1 136 ? -39.810 3.187   40.032  1.00 66.54  ? 136 ASP   B N    1 
ATOM   2866 C  CA   . ASP   B 1 136 ? -38.516 3.875   39.788  1.00 76.60  ? 136 ASP   B CA   1 
ATOM   2867 C  C    . ASP   B 1 136 ? -37.456 2.823   39.459  1.00 69.96  ? 136 ASP   B C    1 
ATOM   2868 O  O    . ASP   B 1 136 ? -36.848 2.231   40.372  1.00 73.04  ? 136 ASP   B O    1 
ATOM   2869 C  CB   . ASP   B 1 136 ? -38.143 4.826   40.920  1.00 86.78  ? 136 ASP   B CB   1 
ATOM   2870 C  CG   . ASP   B 1 136 ? -37.688 6.159   40.351  1.00 97.17  ? 136 ASP   B CG   1 
ATOM   2871 O  OD1  . ASP   B 1 136 ? -36.632 6.182   39.679  1.00 94.13  ? 136 ASP   B OD1  1 
ATOM   2872 O  OD2  . ASP   B 1 136 ? -38.432 7.148   40.521  1.00 107.86 ? 136 ASP   B OD2  1 
ATOM   2873 N  N    . GLN   B 1 137 ? -37.321 2.563   38.171  1.00 57.10  ? 137 GLN   B N    1 
ATOM   2874 C  CA   . GLN   B 1 137 ? -36.439 1.526   37.603  1.00 56.66  ? 137 GLN   B CA   1 
ATOM   2875 C  C    . GLN   B 1 137 ? -35.154 2.223   37.165  1.00 52.94  ? 137 GLN   B C    1 
ATOM   2876 O  O    . GLN   B 1 137 ? -35.149 2.668   36.039  1.00 49.60  ? 137 GLN   B O    1 
ATOM   2877 C  CB   . GLN   B 1 137 ? -37.149 0.899   36.411  1.00 56.67  ? 137 GLN   B CB   1 
ATOM   2878 C  CG   . GLN   B 1 137 ? -36.391 -0.270  35.811  1.00 67.28  ? 137 GLN   B CG   1 
ATOM   2879 C  CD   . GLN   B 1 137 ? -36.532 -1.487  36.681  1.00 60.38  ? 137 GLN   B CD   1 
ATOM   2880 O  OE1  . GLN   B 1 137 ? -37.645 -1.939  36.945  1.00 59.97  ? 137 GLN   B OE1  1 
ATOM   2881 N  NE2  . GLN   B 1 137 ? -35.402 -2.005  37.127  1.00 64.83  ? 137 GLN   B NE2  1 
ATOM   2882 N  N    . LYS   B 1 138 ? -34.139 2.345   38.030  1.00 51.59  ? 138 LYS   B N    1 
ATOM   2883 C  CA   . LYS   B 1 138 ? -33.001 3.287   37.852  1.00 48.09  ? 138 LYS   B CA   1 
ATOM   2884 C  C    . LYS   B 1 138 ? -31.993 2.758   36.827  1.00 50.69  ? 138 LYS   B C    1 
ATOM   2885 O  O    . LYS   B 1 138 ? -31.082 3.496   36.464  1.00 48.41  ? 138 LYS   B O    1 
ATOM   2886 C  CB   . LYS   B 1 138 ? -32.335 3.547   39.202  1.00 53.90  ? 138 LYS   B CB   1 
ATOM   2887 C  CG   . LYS   B 1 138 ? -32.953 4.699   39.973  1.00 55.88  ? 138 LYS   B CG   1 
ATOM   2888 C  CD   . LYS   B 1 138 ? -32.505 4.763   41.390  1.00 64.64  ? 138 LYS   B CD   1 
ATOM   2889 C  CE   . LYS   B 1 138 ? -33.559 5.274   42.356  1.00 69.68  ? 138 LYS   B CE   1 
ATOM   2890 N  NZ   . LYS   B 1 138 ? -33.673 6.750   42.305  1.00 74.92  ? 138 LYS   B NZ   1 
ATOM   2891 N  N    . ASP   B 1 139 ? -32.133 1.518   36.361  1.00 55.23  ? 139 ASP   B N    1 
ATOM   2892 C  CA   . ASP   B 1 139 ? -31.231 0.983   35.308  1.00 54.01  ? 139 ASP   B CA   1 
ATOM   2893 C  C    . ASP   B 1 139 ? -31.920 1.108   33.946  1.00 50.66  ? 139 ASP   B C    1 
ATOM   2894 O  O    . ASP   B 1 139 ? -31.352 0.616   32.970  1.00 42.94  ? 139 ASP   B O    1 
ATOM   2895 C  CB   . ASP   B 1 139 ? -30.763 -0.437  35.628  1.00 54.16  ? 139 ASP   B CB   1 
ATOM   2896 C  CG   . ASP   B 1 139 ? -31.870 -1.402  35.971  1.00 50.94  ? 139 ASP   B CG   1 
ATOM   2897 O  OD1  . ASP   B 1 139 ? -33.021 -0.975  36.006  1.00 54.99  ? 139 ASP   B OD1  1 
ATOM   2898 O  OD2  . ASP   B 1 139 ? -31.552 -2.558  36.222  1.00 56.03  ? 139 ASP   B OD2  1 
ATOM   2899 N  N    . LEU   B 1 140 ? -33.070 1.783   33.882  1.00 48.77  ? 140 LEU   B N    1 
ATOM   2900 C  CA   . LEU   B 1 140 ? -33.708 2.159   32.599  1.00 49.95  ? 140 LEU   B CA   1 
ATOM   2901 C  C    . LEU   B 1 140 ? -33.764 3.682   32.446  1.00 47.60  ? 140 LEU   B C    1 
ATOM   2902 O  O    . LEU   B 1 140 ? -34.026 4.360   33.410  1.00 50.85  ? 140 LEU   B O    1 
ATOM   2903 C  CB   . LEU   B 1 140 ? -35.099 1.539   32.546  1.00 51.42  ? 140 LEU   B CB   1 
ATOM   2904 C  CG   . LEU   B 1 140 ? -35.149 0.039   32.276  1.00 52.31  ? 140 LEU   B CG   1 
ATOM   2905 C  CD1  . LEU   B 1 140 ? -36.586 -0.373  32.050  1.00 53.72  ? 140 LEU   B CD1  1 
ATOM   2906 C  CD2  . LEU   B 1 140 ? -34.300 -0.365  31.082  1.00 53.16  ? 140 LEU   B CD2  1 
ATOM   2907 N  N    . ILE   B 1 141 ? -33.455 4.165   31.250  1.00 49.80  ? 141 ILE   B N    1 
ATOM   2908 C  CA   . ILE   B 1 141 ? -33.718 5.541   30.755  1.00 47.73  ? 141 ILE   B CA   1 
ATOM   2909 C  C    . ILE   B 1 141 ? -35.032 5.468   29.973  1.00 52.45  ? 141 ILE   B C    1 
ATOM   2910 O  O    . ILE   B 1 141 ? -35.039 4.840   28.882  1.00 50.01  ? 141 ILE   B O    1 
ATOM   2911 C  CB   . ILE   B 1 141 ? -32.565 5.991   29.842  1.00 54.59  ? 141 ILE   B CB   1 
ATOM   2912 C  CG1  . ILE   B 1 141 ? -31.219 5.984   30.575  1.00 53.20  ? 141 ILE   B CG1  1 
ATOM   2913 C  CG2  . ILE   B 1 141 ? -32.868 7.346   29.206  1.00 56.63  ? 141 ILE   B CG2  1 
ATOM   2914 C  CD1  . ILE   B 1 141 ? -30.027 5.985   29.643  1.00 53.62  ? 141 ILE   B CD1  1 
ATOM   2915 N  N    . LEU   B 1 142 ? -36.105 6.037   30.524  1.00 50.51  ? 142 LEU   B N    1 
ATOM   2916 C  CA   . LEU   B 1 142 ? -37.417 6.173   29.839  1.00 48.58  ? 142 LEU   B CA   1 
ATOM   2917 C  C    . LEU   B 1 142 ? -37.418 7.485   29.050  1.00 48.37  ? 142 LEU   B C    1 
ATOM   2918 O  O    . LEU   B 1 142 ? -36.812 8.456   29.514  1.00 44.73  ? 142 LEU   B O    1 
ATOM   2919 C  CB   . LEU   B 1 142 ? -38.536 6.120   30.873  1.00 49.58  ? 142 LEU   B CB   1 
ATOM   2920 C  CG   . LEU   B 1 142 ? -38.512 4.890   31.784  1.00 49.04  ? 142 LEU   B CG   1 
ATOM   2921 C  CD1  . LEU   B 1 142 ? -39.644 4.961   32.794  1.00 46.74  ? 142 LEU   B CD1  1 
ATOM   2922 C  CD2  . LEU   B 1 142 ? -38.603 3.606   30.966  1.00 48.58  ? 142 LEU   B CD2  1 
ATOM   2923 N  N    . GLN   B 1 143 ? -37.968 7.448   27.836  1.00 50.94  ? 143 GLN   B N    1 
ATOM   2924 C  CA   . GLN   B 1 143 ? -38.047 8.589   26.883  1.00 49.29  ? 143 GLN   B CA   1 
ATOM   2925 C  C    . GLN   B 1 143 ? -39.470 8.669   26.316  1.00 52.36  ? 143 GLN   B C    1 
ATOM   2926 O  O    . GLN   B 1 143 ? -40.130 7.604   26.139  1.00 45.01  ? 143 GLN   B O    1 
ATOM   2927 C  CB   . GLN   B 1 143 ? -37.052 8.436   25.734  1.00 45.74  ? 143 GLN   B CB   1 
ATOM   2928 C  CG   . GLN   B 1 143 ? -35.640 8.136   26.204  1.00 44.80  ? 143 GLN   B CG   1 
ATOM   2929 C  CD   . GLN   B 1 143 ? -34.677 8.039   25.047  1.00 48.73  ? 143 GLN   B CD   1 
ATOM   2930 O  OE1  . GLN   B 1 143 ? -35.000 7.496   23.976  1.00 47.85  ? 143 GLN   B OE1  1 
ATOM   2931 N  NE2  . GLN   B 1 143 ? -33.490 8.594   25.253  1.00 45.06  ? 143 GLN   B NE2  1 
ATOM   2932 N  N    . GLY   B 1 144 ? -39.914 9.892   26.013  1.00 49.04  ? 144 GLY   B N    1 
ATOM   2933 C  CA   . GLY   B 1 144 ? -41.262 10.128  25.506  1.00 48.07  ? 144 GLY   B CA   1 
ATOM   2934 C  C    . GLY   B 1 144 ? -42.249 9.643   26.538  1.00 52.32  ? 144 GLY   B C    1 
ATOM   2935 O  O    . GLY   B 1 144 ? -42.034 9.942   27.693  1.00 53.49  ? 144 GLY   B O    1 
ATOM   2936 N  N    . ASP   B 1 145 ? -43.249 8.863   26.134  1.00 53.81  ? 145 ASP   B N    1 
ATOM   2937 C  CA   . ASP   B 1 145 ? -44.444 8.599   26.968  1.00 53.81  ? 145 ASP   B CA   1 
ATOM   2938 C  C    . ASP   B 1 145 ? -44.221 7.338   27.807  1.00 51.49  ? 145 ASP   B C    1 
ATOM   2939 O  O    . ASP   B 1 145 ? -45.156 6.980   28.538  1.00 57.54  ? 145 ASP   B O    1 
ATOM   2940 C  CB   . ASP   B 1 145 ? -45.702 8.470   26.093  1.00 56.06  ? 145 ASP   B CB   1 
ATOM   2941 C  CG   . ASP   B 1 145 ? -46.030 9.701   25.248  1.00 61.30  ? 145 ASP   B CG   1 
ATOM   2942 O  OD1  . ASP   B 1 145 ? -45.451 10.785  25.521  1.00 62.00  ? 145 ASP   B OD1  1 
ATOM   2943 O  OD2  . ASP   B 1 145 ? -46.854 9.569   24.294  1.00 59.33  ? 145 ASP   B OD2  1 
ATOM   2944 N  N    . ALA   B 1 146 ? -43.073 6.658   27.671  1.00 48.09  ? 146 ALA   B N    1 
ATOM   2945 C  CA   . ALA   B 1 146 ? -42.826 5.342   28.309  1.00 50.76  ? 146 ALA   B CA   1 
ATOM   2946 C  C    . ALA   B 1 146 ? -42.895 5.505   29.828  1.00 47.23  ? 146 ALA   B C    1 
ATOM   2947 O  O    . ALA   B 1 146 ? -42.365 6.502   30.347  1.00 47.20  ? 146 ALA   B O    1 
ATOM   2948 C  CB   . ALA   B 1 146 ? -41.497 4.769   27.868  1.00 54.61  ? 146 ALA   B CB   1 
ATOM   2949 N  N    . THR   B 1 147 ? -43.508 4.536   30.498  1.00 43.54  ? 147 THR   B N    1 
ATOM   2950 C  CA   . THR   B 1 147 ? -43.631 4.540   31.973  1.00 50.90  ? 147 THR   B CA   1 
ATOM   2951 C  C    . THR   B 1 147 ? -43.503 3.108   32.479  1.00 54.83  ? 147 THR   B C    1 
ATOM   2952 O  O    . THR   B 1 147 ? -43.723 2.196   31.696  1.00 54.38  ? 147 THR   B O    1 
ATOM   2953 C  CB   . THR   B 1 147 ? -44.988 5.076   32.432  1.00 56.03  ? 147 THR   B CB   1 
ATOM   2954 O  OG1  . THR   B 1 147 ? -46.016 4.305   31.821  1.00 62.61  ? 147 THR   B OG1  1 
ATOM   2955 C  CG2  . THR   B 1 147 ? -45.201 6.532   32.103  1.00 54.84  ? 147 THR   B CG2  1 
ATOM   2956 N  N    . THR   B 1 148 ? -43.182 2.948   33.759  1.00 52.96  ? 148 THR   B N    1 
ATOM   2957 C  CA   . THR   B 1 148 ? -43.049 1.609   34.384  1.00 61.91  ? 148 THR   B CA   1 
ATOM   2958 C  C    . THR   B 1 148 ? -43.825 1.578   35.696  1.00 70.21  ? 148 THR   B C    1 
ATOM   2959 O  O    . THR   B 1 148 ? -44.283 2.632   36.133  1.00 64.81  ? 148 THR   B O    1 
ATOM   2960 C  CB   . THR   B 1 148 ? -41.607 1.237   34.746  1.00 56.03  ? 148 THR   B CB   1 
ATOM   2961 O  OG1  . THR   B 1 148 ? -41.090 2.155   35.704  1.00 52.94  ? 148 THR   B OG1  1 
ATOM   2962 C  CG2  . THR   B 1 148 ? -40.683 1.142   33.558  1.00 53.79  ? 148 THR   B CG2  1 
ATOM   2963 N  N    . GLY   B 1 149 ? -43.999 0.378   36.243  1.00 73.27  ? 149 GLY   B N    1 
ATOM   2964 C  CA   . GLY   B 1 149 ? -44.626 0.172   37.558  1.00 90.38  ? 149 GLY   B CA   1 
ATOM   2965 C  C    . GLY   B 1 149 ? -46.101 -0.147  37.517  1.00 99.00  ? 149 GLY   B C    1 
ATOM   2966 O  O    . GLY   B 1 149 ? -46.621 -0.539  38.564  1.00 100.65 ? 149 GLY   B O    1 
ATOM   2967 N  N    . THR   B 1 150 ? -46.747 -0.049  36.359  1.00 102.48 ? 150 THR   B N    1 
ATOM   2968 C  CA   . THR   B 1 150 ? -48.191 -0.372  36.357  1.00 101.93 ? 150 THR   B CA   1 
ATOM   2969 C  C    . THR   B 1 150 ? -48.326 -1.862  36.074  1.00 90.02  ? 150 THR   B C    1 
ATOM   2970 O  O    . THR   B 1 150 ? -48.100 -2.258  34.938  1.00 80.14  ? 150 THR   B O    1 
ATOM   2971 C  CB   . THR   B 1 150 ? -48.966 0.544   35.412  1.00 115.46 ? 150 THR   B CB   1 
ATOM   2972 O  OG1  . THR   B 1 150 ? -49.457 1.604   36.232  1.00 119.67 ? 150 THR   B OG1  1 
ATOM   2973 C  CG2  . THR   B 1 150 ? -50.113 -0.170  34.736  1.00 110.50 ? 150 THR   B CG2  1 
ATOM   2974 N  N    . ASP   B 1 151 ? -48.668 -2.620  37.121  1.00 94.03  ? 151 ASP   B N    1 
ATOM   2975 C  CA   . ASP   B 1 151 ? -48.779 -4.103  37.151  1.00 92.17  ? 151 ASP   B CA   1 
ATOM   2976 C  C    . ASP   B 1 151 ? -47.412 -4.718  36.861  1.00 79.89  ? 151 ASP   B C    1 
ATOM   2977 O  O    . ASP   B 1 151 ? -47.389 -5.781  36.268  1.00 77.51  ? 151 ASP   B O    1 
ATOM   2978 C  CB   . ASP   B 1 151 ? -49.847 -4.641  36.196  1.00 107.46 ? 151 ASP   B CB   1 
ATOM   2979 C  CG   . ASP   B 1 151 ? -50.226 -6.088  36.466  1.00 113.77 ? 151 ASP   B CG   1 
ATOM   2980 O  OD1  . ASP   B 1 151 ? -50.251 -6.480  37.647  1.00 104.74 ? 151 ASP   B OD1  1 
ATOM   2981 O  OD2  . ASP   B 1 151 ? -50.504 -6.810  35.494  1.00 113.99 ? 151 ASP   B OD2  1 
ATOM   2982 N  N    . GLY   B 1 152 ? -46.329 -4.071  37.297  1.00 72.97  ? 152 GLY   B N    1 
ATOM   2983 C  CA   . GLY   B 1 152 ? -44.961 -4.538  37.022  1.00 65.24  ? 152 GLY   B CA   1 
ATOM   2984 C  C    . GLY   B 1 152 ? -44.706 -4.667  35.537  1.00 58.93  ? 152 GLY   B C    1 
ATOM   2985 O  O    . GLY   B 1 152 ? -44.066 -5.623  35.142  1.00 62.69  ? 152 GLY   B O    1 
ATOM   2986 N  N    . ASN   B 1 153 ? -45.178 -3.712  34.749  1.00 51.77  ? 153 ASN   B N    1 
ATOM   2987 C  CA   . ASN   B 1 153 ? -45.017 -3.804  33.283  1.00 56.77  ? 153 ASN   B CA   1 
ATOM   2988 C  C    . ASN   B 1 153 ? -44.463 -2.498  32.729  1.00 48.64  ? 153 ASN   B C    1 
ATOM   2989 O  O    . ASN   B 1 153 ? -44.718 -1.466  33.318  1.00 48.84  ? 153 ASN   B O    1 
ATOM   2990 C  CB   . ASN   B 1 153 ? -46.371 -4.000  32.610  1.00 60.32  ? 153 ASN   B CB   1 
ATOM   2991 C  CG   . ASN   B 1 153 ? -46.913 -5.402  32.725  1.00 60.70  ? 153 ASN   B CG   1 
ATOM   2992 O  OD1  . ASN   B 1 153 ? -46.158 -6.355  32.822  1.00 61.95  ? 153 ASN   B OD1  1 
ATOM   2993 N  ND2  . ASN   B 1 153 ? -48.223 -5.533  32.698  1.00 55.42  ? 153 ASN   B ND2  1 
ATOM   2994 N  N    . LEU   B 1 154 ? -43.691 -2.588  31.656  1.00 42.27  ? 154 LEU   B N    1 
ATOM   2995 C  CA   . LEU   B 1 154 ? -43.214 -1.385  30.918  1.00 45.35  ? 154 LEU   B CA   1 
ATOM   2996 C  C    . LEU   B 1 154 ? -44.292 -1.002  29.888  1.00 46.25  ? 154 LEU   B C    1 
ATOM   2997 O  O    . LEU   B 1 154 ? -44.587 -1.854  29.043  1.00 55.25  ? 154 LEU   B O    1 
ATOM   2998 C  CB   . LEU   B 1 154 ? -41.856 -1.700  30.271  1.00 43.56  ? 154 LEU   B CB   1 
ATOM   2999 C  CG   . LEU   B 1 154 ? -41.337 -0.715  29.213  1.00 43.99  ? 154 LEU   B CG   1 
ATOM   3000 C  CD1  . LEU   B 1 154 ? -41.342 0.724   29.701  1.00 42.53  ? 154 LEU   B CD1  1 
ATOM   3001 C  CD2  . LEU   B 1 154 ? -39.937 -1.096  28.774  1.00 43.46  ? 154 LEU   B CD2  1 
ATOM   3002 N  N    . GLU   B 1 155 ? -44.882 0.208   29.967  1.00 52.21  ? 155 GLU   B N    1 
ATOM   3003 C  CA   . GLU   B 1 155 ? -45.875 0.728   28.966  1.00 47.03  ? 155 GLU   B CA   1 
ATOM   3004 C  C    . GLU   B 1 155 ? -45.146 1.707   28.058  1.00 42.55  ? 155 GLU   B C    1 
ATOM   3005 O  O    . GLU   B 1 155 ? -44.834 2.837   28.494  1.00 44.50  ? 155 GLU   B O    1 
ATOM   3006 C  CB   . GLU   B 1 155 ? -47.098 1.406   29.593  1.00 52.07  ? 155 GLU   B CB   1 
ATOM   3007 C  CG   . GLU   B 1 155 ? -47.916 0.501   30.501  1.00 58.99  ? 155 GLU   B CG   1 
ATOM   3008 C  CD   . GLU   B 1 155 ? -48.835 -0.513  29.829  1.00 66.53  ? 155 GLU   B CD   1 
ATOM   3009 O  OE1  . GLU   B 1 155 ? -48.643 -0.811  28.610  1.00 68.19  ? 155 GLU   B OE1  1 
ATOM   3010 O  OE2  . GLU   B 1 155 ? -49.750 -1.008  30.535  1.00 66.34  ? 155 GLU   B OE2  1 
ATOM   3011 N  N    . LEU   B 1 156 ? -44.784 1.247   26.865  1.00 45.49  ? 156 LEU   B N    1 
ATOM   3012 C  CA   . LEU   B 1 156 ? -43.939 2.048   25.949  1.00 51.94  ? 156 LEU   B CA   1 
ATOM   3013 C  C    . LEU   B 1 156 ? -44.728 3.285   25.505  1.00 56.81  ? 156 LEU   B C    1 
ATOM   3014 O  O    . LEU   B 1 156 ? -44.122 4.382   25.410  1.00 52.25  ? 156 LEU   B O    1 
ATOM   3015 C  CB   . LEU   B 1 156 ? -43.503 1.178   24.773  1.00 47.15  ? 156 LEU   B CB   1 
ATOM   3016 C  CG   . LEU   B 1 156 ? -42.370 0.225   25.105  1.00 44.32  ? 156 LEU   B CG   1 
ATOM   3017 C  CD1  . LEU   B 1 156 ? -42.094 -0.704  23.943  1.00 46.05  ? 156 LEU   B CD1  1 
ATOM   3018 C  CD2  . LEU   B 1 156 ? -41.107 0.986   25.497  1.00 46.79  ? 156 LEU   B CD2  1 
ATOM   3019 N  N    . THR   B 1 157 ? -46.031 3.125   25.272  1.00 52.19  ? 157 THR   B N    1 
ATOM   3020 C  CA   . THR   B 1 157 ? -46.910 4.216   24.793  1.00 51.04  ? 157 THR   B CA   1 
ATOM   3021 C  C    . THR   B 1 157 ? -48.094 4.441   25.737  1.00 54.51  ? 157 THR   B C    1 
ATOM   3022 O  O    . THR   B 1 157 ? -48.462 3.522   26.517  1.00 56.34  ? 157 THR   B O    1 
ATOM   3023 C  CB   . THR   B 1 157 ? -47.371 3.917   23.377  1.00 51.19  ? 157 THR   B CB   1 
ATOM   3024 O  OG1  . THR   B 1 157 ? -48.063 2.664   23.384  1.00 50.00  ? 157 THR   B OG1  1 
ATOM   3025 C  CG2  . THR   B 1 157 ? -46.206 3.923   22.419  1.00 55.01  ? 157 THR   B CG2  1 
ATOM   3026 N  N    . ARG   B 1 158 ? -48.647 5.645   25.641  1.00 53.44  ? 158 ARG   B N    1 
ATOM   3027 C  CA   . ARG   B 1 158 ? -49.634 6.233   26.586  1.00 59.39  ? 158 ARG   B CA   1 
ATOM   3028 C  C    . ARG   B 1 158 ? -50.869 5.321   26.614  1.00 58.69  ? 158 ARG   B C    1 
ATOM   3029 O  O    . ARG   B 1 158 ? -51.355 4.915   25.521  1.00 67.37  ? 158 ARG   B O    1 
ATOM   3030 C  CB   . ARG   B 1 158 ? -49.885 7.695   26.178  1.00 62.87  ? 158 ARG   B CB   1 
ATOM   3031 C  CG   . ARG   B 1 158 ? -50.773 8.492   27.122  1.00 80.98  ? 158 ARG   B CG   1 
ATOM   3032 C  CD   . ARG   B 1 158 ? -50.200 8.734   28.509  1.00 84.68  ? 158 ARG   B CD   1 
ATOM   3033 N  NE   . ARG   B 1 158 ? -48.971 9.513   28.470  1.00 83.97  ? 158 ARG   B NE   1 
ATOM   3034 C  CZ   . ARG   B 1 158 ? -48.024 9.472   29.401  1.00 82.56  ? 158 ARG   B CZ   1 
ATOM   3035 N  NH1  . ARG   B 1 158 ? -48.159 8.694   30.464  1.00 83.68  ? 158 ARG   B NH1  1 
ATOM   3036 N  NH2  . ARG   B 1 158 ? -46.939 10.209  29.260  1.00 75.69  ? 158 ARG   B NH2  1 
ATOM   3037 N  N    . VAL   B 1 159 ? -51.301 4.954   27.822  1.00 61.17  ? 159 VAL   B N    1 
ATOM   3038 C  CA   . VAL   B 1 159 ? -52.551 4.191   28.106  1.00 68.08  ? 159 VAL   B CA   1 
ATOM   3039 C  C    . VAL   B 1 159 ? -53.294 4.940   29.211  1.00 67.51  ? 159 VAL   B C    1 
ATOM   3040 O  O    . VAL   B 1 159 ? -52.651 5.276   30.196  1.00 65.82  ? 159 VAL   B O    1 
ATOM   3041 C  CB   . VAL   B 1 159 ? -52.238 2.740   28.524  1.00 69.98  ? 159 VAL   B CB   1 
ATOM   3042 C  CG1  . VAL   B 1 159 ? -53.511 1.913   28.685  1.00 71.96  ? 159 VAL   B CG1  1 
ATOM   3043 C  CG2  . VAL   B 1 159 ? -51.289 2.070   27.542  1.00 66.95  ? 159 VAL   B CG2  1 
ATOM   3044 N  N    . SER   B 1 160 ? -54.587 5.218   29.043  1.00 73.86  ? 160 SER   B N    1 
ATOM   3045 C  CA   . SER   B 1 160 ? -55.392 5.966   30.048  1.00 75.55  ? 160 SER   B CA   1 
ATOM   3046 C  C    . SER   B 1 160 ? -55.617 5.061   31.269  1.00 72.87  ? 160 SER   B C    1 
ATOM   3047 O  O    . SER   B 1 160 ? -55.310 3.837   31.172  1.00 65.94  ? 160 SER   B O    1 
ATOM   3048 C  CB   . SER   B 1 160 ? -56.694 6.483   29.452  1.00 75.74  ? 160 SER   B CB   1 
ATOM   3049 O  OG   . SER   B 1 160 ? -57.633 5.428   29.251  1.00 73.04  ? 160 SER   B OG   1 
ATOM   3050 N  N    . SER   B 1 161 ? -56.127 5.634   32.368  1.00 79.63  ? 161 SER   B N    1 
ATOM   3051 C  CA   . SER   B 1 161 ? -56.452 4.941   33.651  1.00 88.86  ? 161 SER   B CA   1 
ATOM   3052 C  C    . SER   B 1 161 ? -57.402 3.748   33.428  1.00 94.21  ? 161 SER   B C    1 
ATOM   3053 O  O    . SER   B 1 161 ? -57.264 2.733   34.146  1.00 84.89  ? 161 SER   B O    1 
ATOM   3054 C  CB   . SER   B 1 161 ? -57.036 5.918   34.639  1.00 88.79  ? 161 SER   B CB   1 
ATOM   3055 O  OG   . SER   B 1 161 ? -58.097 6.658   34.047  1.00 97.71  ? 161 SER   B OG   1 
ATOM   3056 N  N    . ASN   B 1 162 ? -58.323 3.848   32.464  1.00 97.93  ? 162 ASN   B N    1 
ATOM   3057 C  CA   . ASN   B 1 162 ? -59.417 2.861   32.252  1.00 99.91  ? 162 ASN   B CA   1 
ATOM   3058 C  C    . ASN   B 1 162 ? -59.040 1.860   31.150  1.00 88.57  ? 162 ASN   B C    1 
ATOM   3059 O  O    . ASN   B 1 162 ? -59.965 1.201   30.638  1.00 86.30  ? 162 ASN   B O    1 
ATOM   3060 C  CB   . ASN   B 1 162 ? -60.736 3.578   31.945  1.00 109.37 ? 162 ASN   B CB   1 
ATOM   3061 C  CG   . ASN   B 1 162 ? -60.616 4.525   30.770  1.00 112.48 ? 162 ASN   B CG   1 
ATOM   3062 O  OD1  . ASN   B 1 162 ? -60.553 4.087   29.622  1.00 106.15 ? 162 ASN   B OD1  1 
ATOM   3063 N  ND2  . ASN   B 1 162 ? -60.552 5.817   31.055  1.00 99.77  ? 162 ASN   B ND2  1 
ATOM   3064 N  N    . GLY   B 1 163 ? -57.756 1.773   30.774  1.00 85.36  ? 163 GLY   B N    1 
ATOM   3065 C  CA   . GLY   B 1 163 ? -57.188 0.656   29.987  1.00 76.78  ? 163 GLY   B CA   1 
ATOM   3066 C  C    . GLY   B 1 163 ? -56.935 0.968   28.510  1.00 77.48  ? 163 GLY   B C    1 
ATOM   3067 O  O    . GLY   B 1 163 ? -56.292 0.128   27.867  1.00 76.37  ? 163 GLY   B O    1 
ATOM   3068 N  N    . SER   B 1 164 ? -57.386 2.110   27.960  1.00 78.95  ? 164 SER   B N    1 
ATOM   3069 C  CA   . SER   B 1 164 ? -57.412 2.351   26.484  1.00 73.53  ? 164 SER   B CA   1 
ATOM   3070 C  C    . SER   B 1 164 ? -56.223 3.190   25.987  1.00 69.01  ? 164 SER   B C    1 
ATOM   3071 O  O    . SER   B 1 164 ? -55.901 4.267   26.512  1.00 59.70  ? 164 SER   B O    1 
ATOM   3072 C  CB   . SER   B 1 164 ? -58.727 2.926   26.029  1.00 68.98  ? 164 SER   B CB   1 
ATOM   3073 O  OG   . SER   B 1 164 ? -58.988 4.124   26.711  1.00 74.10  ? 164 SER   B OG   1 
ATOM   3074 N  N    . PRO   B 1 165 ? -55.561 2.713   24.903  1.00 54.70  ? 165 PRO   B N    1 
ATOM   3075 C  CA   . PRO   B 1 165 ? -54.374 3.355   24.347  1.00 50.08  ? 165 PRO   B CA   1 
ATOM   3076 C  C    . PRO   B 1 165 ? -54.687 4.657   23.593  1.00 50.68  ? 165 PRO   B C    1 
ATOM   3077 O  O    . PRO   B 1 165 ? -55.767 4.788   23.072  1.00 57.08  ? 165 PRO   B O    1 
ATOM   3078 C  CB   . PRO   B 1 165 ? -53.821 2.306   23.364  1.00 50.48  ? 165 PRO   B CB   1 
ATOM   3079 C  CG   . PRO   B 1 165 ? -55.036 1.509   22.924  1.00 49.55  ? 165 PRO   B CG   1 
ATOM   3080 C  CD   . PRO   B 1 165 ? -55.951 1.514   24.137  1.00 55.95  ? 165 PRO   B CD   1 
ATOM   3081 N  N    . GLN   B 1 166 ? -53.704 5.551   23.546  1.00 49.68  ? 166 GLN   B N    1 
ATOM   3082 C  CA   . GLN   B 1 166 ? -53.790 6.907   22.960  1.00 57.33  ? 166 GLN   B CA   1 
ATOM   3083 C  C    . GLN   B 1 166 ? -53.046 6.938   21.616  1.00 56.00  ? 166 GLN   B C    1 
ATOM   3084 O  O    . GLN   B 1 166 ? -52.104 6.129   21.401  1.00 46.59  ? 166 GLN   B O    1 
ATOM   3085 C  CB   . GLN   B 1 166 ? -53.241 7.966   23.925  1.00 59.81  ? 166 GLN   B CB   1 
ATOM   3086 C  CG   . GLN   B 1 166 ? -53.895 7.970   25.313  1.00 67.98  ? 166 GLN   B CG   1 
ATOM   3087 C  CD   . GLN   B 1 166 ? -55.296 8.538   25.393  1.00 68.77  ? 166 GLN   B CD   1 
ATOM   3088 O  OE1  . GLN   B 1 166 ? -56.283 7.804   25.372  1.00 55.15  ? 166 GLN   B OE1  1 
ATOM   3089 N  NE2  . GLN   B 1 166 ? -55.386 9.856   25.528  1.00 76.09  ? 166 GLN   B NE2  1 
ATOM   3090 N  N    . GLY   B 1 167 ? -53.504 7.831   20.732  1.00 49.39  ? 167 GLY   B N    1 
ATOM   3091 C  CA   . GLY   B 1 167 ? -52.964 8.013   19.377  1.00 44.14  ? 167 GLY   B CA   1 
ATOM   3092 C  C    . GLY   B 1 167 ? -51.845 9.016   19.447  1.00 44.82  ? 167 GLY   B C    1 
ATOM   3093 O  O    . GLY   B 1 167 ? -51.762 9.719   20.435  1.00 37.97  ? 167 GLY   B O    1 
ATOM   3094 N  N    . SER   B 1 168 ? -50.954 9.041   18.470  1.00 48.69  ? 168 SER   B N    1 
ATOM   3095 C  CA   . SER   B 1 168 ? -49.893 10.070  18.434  1.00 51.65  ? 168 SER   B CA   1 
ATOM   3096 C  C    . SER   B 1 168 ? -49.034 9.984   19.706  1.00 49.53  ? 168 SER   B C    1 
ATOM   3097 O  O    . SER   B 1 168 ? -48.525 11.033  20.118  1.00 52.59  ? 168 SER   B O    1 
ATOM   3098 C  CB   . SER   B 1 168 ? -50.531 11.429  18.228  1.00 50.99  ? 168 SER   B CB   1 
ATOM   3099 O  OG   . SER   B 1 168 ? -51.262 11.451  16.989  1.00 58.99  ? 168 SER   B OG   1 
ATOM   3100 N  N    . SER   B 1 169 ? -48.847 8.771   20.259  1.00 44.95  ? 169 SER   B N    1 
ATOM   3101 C  CA   . SER   B 1 169 ? -47.909 8.462   21.371  1.00 45.35  ? 169 SER   B CA   1 
ATOM   3102 C  C    . SER   B 1 169 ? -46.625 7.806   20.869  1.00 47.33  ? 169 SER   B C    1 
ATOM   3103 O  O    . SER   B 1 169 ? -46.688 6.993   19.937  1.00 48.60  ? 169 SER   B O    1 
ATOM   3104 C  CB   . SER   B 1 169 ? -48.536 7.584   22.377  1.00 49.11  ? 169 SER   B CB   1 
ATOM   3105 O  OG   . SER   B 1 169 ? -47.730 7.564   23.531  1.00 45.18  ? 169 SER   B OG   1 
ATOM   3106 N  N    . VAL   B 1 170 ? -45.506 8.122   21.513  1.00 48.60  ? 170 VAL   B N    1 
ATOM   3107 C  CA   . VAL   B 1 170 ? -44.181 7.505   21.224  1.00 49.57  ? 170 VAL   B CA   1 
ATOM   3108 C  C    . VAL   B 1 170 ? -43.363 7.447   22.522  1.00 47.99  ? 170 VAL   B C    1 
ATOM   3109 O  O    . VAL   B 1 170 ? -43.283 8.460   23.234  1.00 56.29  ? 170 VAL   B O    1 
ATOM   3110 C  CB   . VAL   B 1 170 ? -43.481 8.288   20.098  1.00 51.32  ? 170 VAL   B CB   1 
ATOM   3111 C  CG1  . VAL   B 1 170 ? -43.237 9.727   20.499  1.00 51.28  ? 170 VAL   B CG1  1 
ATOM   3112 C  CG2  . VAL   B 1 170 ? -42.194 7.632   19.627  1.00 45.62  ? 170 VAL   B CG2  1 
ATOM   3113 N  N    . GLY   B 1 171 ? -42.815 6.276   22.837  1.00 50.19  ? 171 GLY   B N    1 
ATOM   3114 C  CA   . GLY   B 1 171 ? -42.000 6.037   24.041  1.00 54.41  ? 171 GLY   B CA   1 
ATOM   3115 C  C    . GLY   B 1 171 ? -40.905 5.003   23.821  1.00 51.40  ? 171 GLY   B C    1 
ATOM   3116 O  O    . GLY   B 1 171 ? -41.072 4.142   22.959  1.00 49.55  ? 171 GLY   B O    1 
ATOM   3117 N  N    . ARG   B 1 172 ? -39.808 5.114   24.574  1.00 45.58  ? 172 ARG   B N    1 
ATOM   3118 C  CA   . ARG   B 1 172 ? -38.684 4.151   24.547  1.00 46.08  ? 172 ARG   B CA   1 
ATOM   3119 C  C    . ARG   B 1 172 ? -38.136 3.895   25.965  1.00 49.45  ? 172 ARG   B C    1 
ATOM   3120 O  O    . ARG   B 1 172 ? -38.300 4.747   26.878  1.00 47.44  ? 172 ARG   B O    1 
ATOM   3121 C  CB   . ARG   B 1 172 ? -37.577 4.653   23.618  1.00 42.49  ? 172 ARG   B CB   1 
ATOM   3122 C  CG   . ARG   B 1 172 ? -38.098 5.075   22.261  1.00 44.87  ? 172 ARG   B CG   1 
ATOM   3123 C  CD   . ARG   B 1 172 ? -37.059 5.407   21.200  1.00 45.65  ? 172 ARG   B CD   1 
ATOM   3124 N  NE   . ARG   B 1 172 ? -35.798 5.981   21.636  1.00 45.95  ? 172 ARG   B NE   1 
ATOM   3125 C  CZ   . ARG   B 1 172 ? -34.762 6.234   20.832  1.00 49.72  ? 172 ARG   B CZ   1 
ATOM   3126 N  NH1  . ARG   B 1 172 ? -34.857 6.041   19.523  1.00 55.06  ? 172 ARG   B NH1  1 
ATOM   3127 N  NH2  . ARG   B 1 172 ? -33.634 6.703   21.344  1.00 49.46  ? 172 ARG   B NH2  1 
ATOM   3128 N  N    . ALA   B 1 173 ? -37.491 2.740   26.132  1.00 47.63  ? 173 ALA   B N    1 
ATOM   3129 C  CA   . ALA   B 1 173 ? -36.767 2.326   27.350  1.00 47.82  ? 173 ALA   B CA   1 
ATOM   3130 C  C    . ALA   B 1 173 ? -35.395 1.818   26.914  1.00 47.43  ? 173 ALA   B C    1 
ATOM   3131 O  O    . ALA   B 1 173 ? -35.355 0.919   26.043  1.00 46.72  ? 173 ALA   B O    1 
ATOM   3132 C  CB   . ALA   B 1 173 ? -37.556 1.260   28.068  1.00 53.49  ? 173 ALA   B CB   1 
ATOM   3133 N  N    . LEU   B 1 174 ? -34.326 2.424   27.433  1.00 46.11  ? 174 LEU   B N    1 
ATOM   3134 C  CA   . LEU   B 1 174 ? -32.934 2.003   27.158  1.00 46.53  ? 174 LEU   B CA   1 
ATOM   3135 C  C    . LEU   B 1 174 ? -32.295 1.410   28.421  1.00 48.33  ? 174 LEU   B C    1 
ATOM   3136 O  O    . LEU   B 1 174 ? -32.592 1.904   29.549  1.00 48.33  ? 174 LEU   B O    1 
ATOM   3137 C  CB   . LEU   B 1 174 ? -32.151 3.204   26.649  1.00 48.80  ? 174 LEU   B CB   1 
ATOM   3138 C  CG   . LEU   B 1 174 ? -32.620 3.758   25.308  1.00 49.84  ? 174 LEU   B CG   1 
ATOM   3139 C  CD1  . LEU   B 1 174 ? -33.568 4.925   25.510  1.00 49.84  ? 174 LEU   B CD1  1 
ATOM   3140 C  CD2  . LEU   B 1 174 ? -31.429 4.207   24.488  1.00 49.04  ? 174 LEU   B CD2  1 
ATOM   3141 N  N    . PHE   B 1 175 ? -31.480 0.364   28.255  1.00 45.77  ? 175 PHE   B N    1 
ATOM   3142 C  CA   . PHE   B 1 175 ? -30.658 -0.139  29.377  1.00 50.29  ? 175 PHE   B CA   1 
ATOM   3143 C  C    . PHE   B 1 175 ? -29.672 0.976   29.687  1.00 44.68  ? 175 PHE   B C    1 
ATOM   3144 O  O    . PHE   B 1 175 ? -29.152 1.646   28.777  1.00 44.41  ? 175 PHE   B O    1 
ATOM   3145 C  CB   . PHE   B 1 175 ? -29.971 -1.483  29.131  1.00 47.48  ? 175 PHE   B CB   1 
ATOM   3146 C  CG   . PHE   B 1 175 ? -29.346 -2.016  30.394  1.00 45.70  ? 175 PHE   B CG   1 
ATOM   3147 C  CD1  . PHE   B 1 175 ? -30.143 -2.380  31.473  1.00 50.21  ? 175 PHE   B CD1  1 
ATOM   3148 C  CD2  . PHE   B 1 175 ? -27.964 -2.125  30.527  1.00 45.75  ? 175 PHE   B CD2  1 
ATOM   3149 C  CE1  . PHE   B 1 175 ? -29.577 -2.842  32.658  1.00 50.11  ? 175 PHE   B CE1  1 
ATOM   3150 C  CE2  . PHE   B 1 175 ? -27.400 -2.600  31.705  1.00 45.58  ? 175 PHE   B CE2  1 
ATOM   3151 C  CZ   . PHE   B 1 175 ? -28.204 -2.938  32.774  1.00 45.81  ? 175 PHE   B CZ   1 
ATOM   3152 N  N    . TYR   B 1 176 ? -29.486 1.226   30.968  1.00 49.91  ? 176 TYR   B N    1 
ATOM   3153 C  CA   . TYR   B 1 176 ? -28.717 2.398   31.450  1.00 54.95  ? 176 TYR   B CA   1 
ATOM   3154 C  C    . TYR   B 1 176 ? -27.283 2.314   30.940  1.00 54.08  ? 176 TYR   B C    1 
ATOM   3155 O  O    . TYR   B 1 176 ? -26.723 3.361   30.586  1.00 53.29  ? 176 TYR   B O    1 
ATOM   3156 C  CB   . TYR   B 1 176 ? -28.753 2.502   32.971  1.00 56.39  ? 176 TYR   B CB   1 
ATOM   3157 C  CG   . TYR   B 1 176 ? -28.253 3.831   33.451  1.00 63.81  ? 176 TYR   B CG   1 
ATOM   3158 C  CD1  . TYR   B 1 176 ? -29.096 4.924   33.543  1.00 67.48  ? 176 TYR   B CD1  1 
ATOM   3159 C  CD2  . TYR   B 1 176 ? -26.922 3.997   33.774  1.00 62.16  ? 176 TYR   B CD2  1 
ATOM   3160 C  CE1  . TYR   B 1 176 ? -28.630 6.149   33.982  1.00 69.72  ? 176 TYR   B CE1  1 
ATOM   3161 C  CE2  . TYR   B 1 176 ? -26.441 5.216   34.209  1.00 72.09  ? 176 TYR   B CE2  1 
ATOM   3162 C  CZ   . TYR   B 1 176 ? -27.293 6.295   34.313  1.00 66.97  ? 176 TYR   B CZ   1 
ATOM   3163 O  OH   . TYR   B 1 176 ? -26.764 7.485   34.712  1.00 61.97  ? 176 TYR   B OH   1 
ATOM   3164 N  N    . ALA   B 1 177 ? -26.714 1.106   30.930  1.00 56.38  ? 177 ALA   B N    1 
ATOM   3165 C  CA   . ALA   B 1 177 ? -25.263 0.878   30.774  1.00 54.45  ? 177 ALA   B CA   1 
ATOM   3166 C  C    . ALA   B 1 177 ? -24.984 0.718   29.301  1.00 46.80  ? 177 ALA   B C    1 
ATOM   3167 O  O    . ALA   B 1 177 ? -25.677 -0.036  28.641  1.00 42.06  ? 177 ALA   B O    1 
ATOM   3168 C  CB   . ALA   B 1 177 ? -24.801 -0.330  31.543  1.00 57.02  ? 177 ALA   B CB   1 
ATOM   3169 N  N    . PRO   B 1 178 ? -23.984 1.450   28.772  1.00 50.38  ? 178 PRO   B N    1 
ATOM   3170 C  CA   . PRO   B 1 178 ? -23.454 1.188   27.436  1.00 50.85  ? 178 PRO   B CA   1 
ATOM   3171 C  C    . PRO   B 1 178 ? -22.923 -0.248  27.327  1.00 47.68  ? 178 PRO   B C    1 
ATOM   3172 O  O    . PRO   B 1 178 ? -22.484 -0.778  28.290  1.00 48.86  ? 178 PRO   B O    1 
ATOM   3173 C  CB   . PRO   B 1 178 ? -22.296 2.186   27.273  1.00 51.06  ? 178 PRO   B CB   1 
ATOM   3174 C  CG   . PRO   B 1 178 ? -22.589 3.272   28.289  1.00 52.70  ? 178 PRO   B CG   1 
ATOM   3175 C  CD   . PRO   B 1 178 ? -23.310 2.581   29.434  1.00 50.70  ? 178 PRO   B CD   1 
ATOM   3176 N  N    . VAL   B 1 179 ? -22.979 -0.811  26.133  1.00 49.13  ? 179 VAL   B N    1 
ATOM   3177 C  CA   . VAL   B 1 179 ? -22.594 -2.213  25.820  1.00 48.70  ? 179 VAL   B CA   1 
ATOM   3178 C  C    . VAL   B 1 179 ? -21.457 -2.192  24.799  1.00 48.14  ? 179 VAL   B C    1 
ATOM   3179 O  O    . VAL   B 1 179 ? -21.542 -1.444  23.797  1.00 52.93  ? 179 VAL   B O    1 
ATOM   3180 C  CB   . VAL   B 1 179 ? -23.824 -2.982  25.305  1.00 51.92  ? 179 VAL   B CB   1 
ATOM   3181 C  CG1  . VAL   B 1 179 ? -23.516 -4.453  25.081  1.00 51.73  ? 179 VAL   B CG1  1 
ATOM   3182 C  CG2  . VAL   B 1 179 ? -25.006 -2.801  26.259  1.00 50.47  ? 179 VAL   B CG2  1 
ATOM   3183 N  N    . HIS   B 1 180 ? -20.398 -2.941  25.075  1.00 50.22  ? 180 HIS   B N    1 
ATOM   3184 C  CA   . HIS   B 1 180 ? -19.271 -3.129  24.134  1.00 51.68  ? 180 HIS   B CA   1 
ATOM   3185 C  C    . HIS   B 1 180 ? -19.807 -4.151  23.145  1.00 50.68  ? 180 HIS   B C    1 
ATOM   3186 O  O    . HIS   B 1 180 ? -19.996 -5.288  23.575  1.00 56.11  ? 180 HIS   B O    1 
ATOM   3187 C  CB   . HIS   B 1 180 ? -17.990 -3.548  24.880  1.00 48.56  ? 180 HIS   B CB   1 
ATOM   3188 C  CG   . HIS   B 1 180 ? -16.723 -3.121  24.203  1.00 56.51  ? 180 HIS   B CG   1 
ATOM   3189 N  ND1  . HIS   B 1 180 ? -15.476 -3.220  24.809  1.00 61.00  ? 180 HIS   B ND1  1 
ATOM   3190 C  CD2  . HIS   B 1 180 ? -16.500 -2.569  22.990  1.00 57.32  ? 180 HIS   B CD2  1 
ATOM   3191 C  CE1  . HIS   B 1 180 ? -14.552 -2.750  23.996  1.00 59.82  ? 180 HIS   B CE1  1 
ATOM   3192 N  NE2  . HIS   B 1 180 ? -15.154 -2.371  22.869  1.00 62.35  ? 180 HIS   B NE2  1 
ATOM   3193 N  N    . ILE   B 1 181 ? -20.209 -3.743  21.943  1.00 55.01  ? 181 ILE   B N    1 
ATOM   3194 C  CA   . ILE   B 1 181 ? -21.021 -4.651  21.073  1.00 57.86  ? 181 ILE   B CA   1 
ATOM   3195 C  C    . ILE   B 1 181 ? -20.086 -5.356  20.089  1.00 54.77  ? 181 ILE   B C    1 
ATOM   3196 O  O    . ILE   B 1 181 ? -20.335 -6.514  19.759  1.00 58.41  ? 181 ILE   B O    1 
ATOM   3197 C  CB   . ILE   B 1 181 ? -22.211 -3.913  20.420  1.00 56.58  ? 181 ILE   B CB   1 
ATOM   3198 C  CG1  . ILE   B 1 181 ? -23.339 -4.883  20.049  1.00 62.56  ? 181 ILE   B CG1  1 
ATOM   3199 C  CG2  . ILE   B 1 181 ? -21.803 -3.079  19.225  1.00 51.65  ? 181 ILE   B CG2  1 
ATOM   3200 C  CD1  . ILE   B 1 181 ? -24.099 -5.471  21.228  1.00 59.98  ? 181 ILE   B CD1  1 
ATOM   3201 N  N    . TRP   B 1 182 ? -19.005 -4.697  19.700  1.00 60.13  ? 182 TRP   B N    1 
ATOM   3202 C  CA   . TRP   B 1 182 ? -17.916 -5.316  18.913  1.00 64.86  ? 182 TRP   B CA   1 
ATOM   3203 C  C    . TRP   B 1 182 ? -16.565 -4.771  19.382  1.00 64.68  ? 182 TRP   B C    1 
ATOM   3204 O  O    . TRP   B 1 182 ? -16.476 -3.615  19.857  1.00 64.39  ? 182 TRP   B O    1 
ATOM   3205 C  CB   . TRP   B 1 182 ? -18.130 -5.130  17.398  1.00 75.37  ? 182 TRP   B CB   1 
ATOM   3206 C  CG   . TRP   B 1 182 ? -18.046 -3.729  16.851  1.00 79.39  ? 182 TRP   B CG   1 
ATOM   3207 C  CD1  . TRP   B 1 182 ? -19.081 -2.849  16.716  1.00 78.24  ? 182 TRP   B CD1  1 
ATOM   3208 C  CD2  . TRP   B 1 182 ? -16.895 -3.066  16.281  1.00 78.83  ? 182 TRP   B CD2  1 
ATOM   3209 N  NE1  . TRP   B 1 182 ? -18.650 -1.684  16.142  1.00 80.89  ? 182 TRP   B NE1  1 
ATOM   3210 C  CE2  . TRP   B 1 182 ? -17.316 -1.783  15.865  1.00 78.07  ? 182 TRP   B CE2  1 
ATOM   3211 C  CE3  . TRP   B 1 182 ? -15.554 -3.416  16.085  1.00 81.31  ? 182 TRP   B CE3  1 
ATOM   3212 C  CZ2  . TRP   B 1 182 ? -16.452 -0.858  15.281  1.00 78.93  ? 182 TRP   B CZ2  1 
ATOM   3213 C  CZ3  . TRP   B 1 182 ? -14.699 -2.501  15.505  1.00 83.86  ? 182 TRP   B CZ3  1 
ATOM   3214 C  CH2  . TRP   B 1 182 ? -15.142 -1.238  15.111  1.00 77.88  ? 182 TRP   B CH2  1 
ATOM   3215 N  N    . GLU   B 1 183 ? -15.553 -5.613  19.239  1.00 68.93  ? 183 GLU   B N    1 
ATOM   3216 C  CA   . GLU   B 1 183 ? -14.120 -5.281  19.390  1.00 80.66  ? 183 GLU   B CA   1 
ATOM   3217 C  C    . GLU   B 1 183 ? -13.428 -5.945  18.206  1.00 84.75  ? 183 GLU   B C    1 
ATOM   3218 O  O    . GLU   B 1 183 ? -13.851 -7.075  17.873  1.00 84.60  ? 183 GLU   B O    1 
ATOM   3219 C  CB   . GLU   B 1 183 ? -13.635 -5.821  20.734  1.00 84.57  ? 183 GLU   B CB   1 
ATOM   3220 C  CG   . GLU   B 1 183 ? -12.448 -5.086  21.312  1.00 88.09  ? 183 GLU   B CG   1 
ATOM   3221 C  CD   . GLU   B 1 183 ? -12.296 -5.337  22.801  1.00 93.38  ? 183 GLU   B CD   1 
ATOM   3222 O  OE1  . GLU   B 1 183 ? -12.794 -6.397  23.274  1.00 84.36  ? 183 GLU   B OE1  1 
ATOM   3223 O  OE2  . GLU   B 1 183 ? -11.699 -4.470  23.485  1.00 94.81  ? 183 GLU   B OE2  1 
ATOM   3224 N  N    . SER   B 1 184 ? -12.453 -5.289  17.569  1.00 89.98  ? 184 SER   B N    1 
ATOM   3225 C  CA   . SER   B 1 184 ? -11.729 -5.889  16.416  1.00 90.33  ? 184 SER   B CA   1 
ATOM   3226 C  C    . SER   B 1 184 ? -10.894 -7.087  16.907  1.00 89.93  ? 184 SER   B C    1 
ATOM   3227 O  O    . SER   B 1 184 ? -10.783 -8.063  16.147  1.00 85.05  ? 184 SER   B O    1 
ATOM   3228 C  CB   . SER   B 1 184 ? -10.905 -4.884  15.664  1.00 85.27  ? 184 SER   B CB   1 
ATOM   3229 O  OG   . SER   B 1 184 ? -10.360 -5.487  14.500  1.00 89.72  ? 184 SER   B OG   1 
ATOM   3230 N  N    . SER   B 1 185 ? -10.432 -7.050  18.166  1.00 79.07  ? 185 SER   B N    1 
ATOM   3231 C  CA   . SER   B 1 185 ? -9.462  -7.989  18.794  1.00 77.99  ? 185 SER   B CA   1 
ATOM   3232 C  C    . SER   B 1 185 ? -10.125 -9.282  19.291  1.00 76.69  ? 185 SER   B C    1 
ATOM   3233 O  O    . SER   B 1 185 ? -9.445  -10.040 20.014  1.00 82.53  ? 185 SER   B O    1 
ATOM   3234 C  CB   . SER   B 1 185 ? -8.801  -7.305  19.960  1.00 80.90  ? 185 SER   B CB   1 
ATOM   3235 O  OG   . SER   B 1 185 ? -9.731  -7.183  21.036  1.00 74.42  ? 185 SER   B OG   1 
ATOM   3236 N  N    . ALA   B 1 186 ? -11.408 -9.505  19.003  1.00 72.14  ? 186 ALA   B N    1 
ATOM   3237 C  CA   . ALA   B 1 186 ? -12.204 -10.638 19.538  1.00 66.35  ? 186 ALA   B CA   1 
ATOM   3238 C  C    . ALA   B 1 186 ? -12.443 -11.660 18.427  1.00 63.01  ? 186 ALA   B C    1 
ATOM   3239 O  O    . ALA   B 1 186 ? -12.566 -11.246 17.271  1.00 62.01  ? 186 ALA   B O    1 
ATOM   3240 C  CB   . ALA   B 1 186 ? -13.513 -10.130 20.087  1.00 64.74  ? 186 ALA   B CB   1 
ATOM   3241 N  N    . VAL   B 1 187 ? -12.512 -12.944 18.772  1.00 66.31  ? 187 VAL   B N    1 
ATOM   3242 C  CA   . VAL   B 1 187 ? -12.733 -14.050 17.792  1.00 71.45  ? 187 VAL   B CA   1 
ATOM   3243 C  C    . VAL   B 1 187 ? -14.243 -14.293 17.637  1.00 65.94  ? 187 VAL   B C    1 
ATOM   3244 O  O    . VAL   B 1 187 ? -14.651 -14.655 16.522  1.00 77.89  ? 187 VAL   B O    1 
ATOM   3245 C  CB   . VAL   B 1 187 ? -11.948 -15.326 18.169  1.00 69.17  ? 187 VAL   B CB   1 
ATOM   3246 C  CG1  . VAL   B 1 187 ? -10.468 -15.014 18.375  1.00 78.64  ? 187 VAL   B CG1  1 
ATOM   3247 C  CG2  . VAL   B 1 187 ? -12.510 -16.027 19.393  1.00 67.14  ? 187 VAL   B CG2  1 
ATOM   3248 N  N    . VAL   B 1 188 ? -15.044 -14.096 18.691  1.00 63.39  ? 188 VAL   B N    1 
ATOM   3249 C  CA   . VAL   B 1 188 ? -16.530 -14.247 18.623  1.00 67.00  ? 188 VAL   B CA   1 
ATOM   3250 C  C    . VAL   B 1 188 ? -17.157 -13.144 19.486  1.00 64.46  ? 188 VAL   B C    1 
ATOM   3251 O  O    . VAL   B 1 188 ? -16.856 -13.088 20.674  1.00 65.26  ? 188 VAL   B O    1 
ATOM   3252 C  CB   . VAL   B 1 188 ? -17.004 -15.679 18.983  1.00 68.19  ? 188 VAL   B CB   1 
ATOM   3253 C  CG1  . VAL   B 1 188 ? -16.295 -16.251 20.186  1.00 73.09  ? 188 VAL   B CG1  1 
ATOM   3254 C  CG2  . VAL   B 1 188 ? -18.514 -15.788 19.183  1.00 69.77  ? 188 VAL   B CG2  1 
ATOM   3255 N  N    . ALA   B 1 189 ? -17.911 -12.243 18.849  1.00 60.41  ? 189 ALA   B N    1 
ATOM   3256 C  CA   . ALA   B 1 189 ? -18.860 -11.287 19.467  1.00 62.82  ? 189 ALA   B CA   1 
ATOM   3257 C  C    . ALA   B 1 189 ? -20.269 -11.842 19.221  1.00 60.35  ? 189 ALA   B C    1 
ATOM   3258 O  O    . ALA   B 1 189 ? -20.524 -12.358 18.113  1.00 63.90  ? 189 ALA   B O    1 
ATOM   3259 C  CB   . ALA   B 1 189 ? -18.694 -9.874  18.915  1.00 54.23  ? 189 ALA   B CB   1 
ATOM   3260 N  N    . SER   B 1 190 ? -21.131 -11.810 20.233  1.00 53.97  ? 190 SER   B N    1 
ATOM   3261 C  CA   . SER   B 1 190 ? -22.509 -12.327 20.120  1.00 54.47  ? 190 SER   B CA   1 
ATOM   3262 C  C    . SER   B 1 190 ? -23.406 -11.549 21.075  1.00 47.51  ? 190 SER   B C    1 
ATOM   3263 O  O    . SER   B 1 190 ? -22.901 -11.059 22.067  1.00 48.87  ? 190 SER   B O    1 
ATOM   3264 C  CB   . SER   B 1 190 ? -22.557 -13.839 20.333  1.00 53.05  ? 190 SER   B CB   1 
ATOM   3265 O  OG   . SER   B 1 190 ? -22.566 -14.204 21.707  1.00 57.48  ? 190 SER   B OG   1 
ATOM   3266 N  N    . PHE   B 1 191 ? -24.692 -11.464 20.766  1.00 44.43  ? 191 PHE   B N    1 
ATOM   3267 C  CA   . PHE   B 1 191 ? -25.723 -10.970 21.707  1.00 47.79  ? 191 PHE   B CA   1 
ATOM   3268 C  C    . PHE   B 1 191 ? -27.034 -11.687 21.443  1.00 44.76  ? 191 PHE   B C    1 
ATOM   3269 O  O    . PHE   B 1 191 ? -27.191 -12.288 20.374  1.00 47.14  ? 191 PHE   B O    1 
ATOM   3270 C  CB   . PHE   B 1 191 ? -25.928 -9.449  21.621  1.00 50.75  ? 191 PHE   B CB   1 
ATOM   3271 C  CG   . PHE   B 1 191 ? -26.450 -8.893  20.319  1.00 48.59  ? 191 PHE   B CG   1 
ATOM   3272 C  CD1  . PHE   B 1 191 ? -27.804 -8.888  20.036  1.00 52.84  ? 191 PHE   B CD1  1 
ATOM   3273 C  CD2  . PHE   B 1 191 ? -25.595 -8.291  19.410  1.00 48.77  ? 191 PHE   B CD2  1 
ATOM   3274 C  CE1  . PHE   B 1 191 ? -28.280 -8.347  18.847  1.00 54.44  ? 191 PHE   B CE1  1 
ATOM   3275 C  CE2  . PHE   B 1 191 ? -26.078 -7.729  18.235  1.00 48.68  ? 191 PHE   B CE2  1 
ATOM   3276 C  CZ   . PHE   B 1 191 ? -27.416 -7.744  17.961  1.00 48.03  ? 191 PHE   B CZ   1 
ATOM   3277 N  N    . GLU   B 1 192 ? -27.956 -11.552 22.392  1.00 48.12  ? 192 GLU   B N    1 
ATOM   3278 C  CA   . GLU   B 1 192 ? -29.268 -12.242 22.413  1.00 48.12  ? 192 GLU   B CA   1 
ATOM   3279 C  C    . GLU   B 1 192 ? -30.188 -11.355 23.253  1.00 51.96  ? 192 GLU   B C    1 
ATOM   3280 O  O    . GLU   B 1 192 ? -29.716 -10.783 24.275  1.00 49.13  ? 192 GLU   B O    1 
ATOM   3281 C  CB   . GLU   B 1 192 ? -29.004 -13.671 22.864  1.00 57.83  ? 192 GLU   B CB   1 
ATOM   3282 C  CG   . GLU   B 1 192 ? -30.129 -14.362 23.609  1.00 75.37  ? 192 GLU   B CG   1 
ATOM   3283 C  CD   . GLU   B 1 192 ? -29.636 -15.631 24.303  1.00 79.64  ? 192 GLU   B CD   1 
ATOM   3284 O  OE1  . GLU   B 1 192 ? -28.450 -15.667 24.665  1.00 82.45  ? 192 GLU   B OE1  1 
ATOM   3285 O  OE2  . GLU   B 1 192 ? -30.426 -16.582 24.475  1.00 95.44  ? 192 GLU   B OE2  1 
ATOM   3286 N  N    . ALA   B 1 193 ? -31.393 -11.111 22.748  1.00 40.68  ? 193 ALA   B N    1 
ATOM   3287 C  CA   . ALA   B 1 193 ? -32.436 -10.366 23.456  1.00 46.67  ? 193 ALA   B CA   1 
ATOM   3288 C  C    . ALA   B 1 193 ? -33.730 -11.159 23.345  1.00 46.48  ? 193 ALA   B C    1 
ATOM   3289 O  O    . ALA   B 1 193 ? -33.951 -11.828 22.329  1.00 47.55  ? 193 ALA   B O    1 
ATOM   3290 C  CB   . ALA   B 1 193 ? -32.570 -8.976  22.860  1.00 48.51  ? 193 ALA   B CB   1 
ATOM   3291 N  N    . THR   B 1 194 ? -34.570 -11.039 24.356  1.00 48.93  ? 194 THR   B N    1 
ATOM   3292 C  CA   . THR   B 1 194 ? -35.859 -11.756 24.488  1.00 45.10  ? 194 THR   B CA   1 
ATOM   3293 C  C    . THR   B 1 194 ? -36.797 -10.761 25.161  1.00 43.38  ? 194 THR   B C    1 
ATOM   3294 O  O    . THR   B 1 194 ? -36.352 -10.036 26.059  1.00 44.51  ? 194 THR   B O    1 
ATOM   3295 C  CB   . THR   B 1 194 ? -35.656 -13.076 25.251  1.00 49.90  ? 194 THR   B CB   1 
ATOM   3296 O  OG1  . THR   B 1 194 ? -34.774 -13.881 24.462  1.00 56.96  ? 194 THR   B OG1  1 
ATOM   3297 C  CG2  . THR   B 1 194 ? -36.926 -13.863 25.520  1.00 45.65  ? 194 THR   B CG2  1 
ATOM   3298 N  N    . PHE   B 1 195 ? -38.018 -10.640 24.689  1.00 38.11  ? 195 PHE   B N    1 
ATOM   3299 C  CA   . PHE   B 1 195 ? -39.017 -9.840  25.410  1.00 41.75  ? 195 PHE   B CA   1 
ATOM   3300 C  C    . PHE   B 1 195 ? -40.378 -10.448 25.144  1.00 44.88  ? 195 PHE   B C    1 
ATOM   3301 O  O    . PHE   B 1 195 ? -40.582 -11.092 24.097  1.00 44.17  ? 195 PHE   B O    1 
ATOM   3302 C  CB   . PHE   B 1 195 ? -38.911 -8.353  25.059  1.00 45.89  ? 195 PHE   B CB   1 
ATOM   3303 C  CG   . PHE   B 1 195 ? -39.120 -7.970  23.618  1.00 44.33  ? 195 PHE   B CG   1 
ATOM   3304 C  CD1  . PHE   B 1 195 ? -38.081 -8.029  22.706  1.00 48.65  ? 195 PHE   B CD1  1 
ATOM   3305 C  CD2  . PHE   B 1 195 ? -40.353 -7.525  23.180  1.00 44.85  ? 195 PHE   B CD2  1 
ATOM   3306 C  CE1  . PHE   B 1 195 ? -38.291 -7.666  21.384  1.00 50.58  ? 195 PHE   B CE1  1 
ATOM   3307 C  CE2  . PHE   B 1 195 ? -40.554 -7.154  21.862  1.00 42.72  ? 195 PHE   B CE2  1 
ATOM   3308 C  CZ   . PHE   B 1 195 ? -39.529 -7.230  20.968  1.00 44.11  ? 195 PHE   B CZ   1 
ATOM   3309 N  N    . THR   B 1 196 ? -41.263 -10.275 26.114  1.00 41.98  ? 196 THR   B N    1 
ATOM   3310 C  CA   . THR   B 1 196 ? -42.660 -10.719 25.994  1.00 46.17  ? 196 THR   B CA   1 
ATOM   3311 C  C    . THR   B 1 196 ? -43.489 -9.438  25.980  1.00 47.40  ? 196 THR   B C    1 
ATOM   3312 O  O    . THR   B 1 196 ? -43.119 -8.491  26.693  1.00 48.39  ? 196 THR   B O    1 
ATOM   3313 C  CB   . THR   B 1 196 ? -43.002 -11.736 27.086  1.00 39.23  ? 196 THR   B CB   1 
ATOM   3314 O  OG1  . THR   B 1 196 ? -42.730 -11.038 28.292  1.00 40.86  ? 196 THR   B OG1  1 
ATOM   3315 C  CG2  . THR   B 1 196 ? -42.189 -13.007 27.015  1.00 38.12  ? 196 THR   B CG2  1 
ATOM   3316 N  N    . PHE   B 1 197 ? -44.511 -9.401  25.134  1.00 45.30  ? 197 PHE   B N    1 
ATOM   3317 C  CA   . PHE   B 1 197 ? -45.315 -8.190  24.866  1.00 46.52  ? 197 PHE   B CA   1 
ATOM   3318 C  C    . PHE   B 1 197 ? -46.784 -8.595  24.773  1.00 53.01  ? 197 PHE   B C    1 
ATOM   3319 O  O    . PHE   B 1 197 ? -47.111 -9.797  24.511  1.00 47.75  ? 197 PHE   B O    1 
ATOM   3320 C  CB   . PHE   B 1 197 ? -44.803 -7.517  23.593  1.00 44.12  ? 197 PHE   B CB   1 
ATOM   3321 C  CG   . PHE   B 1 197 ? -44.843 -8.430  22.402  1.00 45.45  ? 197 PHE   B CG   1 
ATOM   3322 C  CD1  . PHE   B 1 197 ? -46.010 -8.548  21.652  1.00 45.31  ? 197 PHE   B CD1  1 
ATOM   3323 C  CD2  . PHE   B 1 197 ? -43.746 -9.214  22.073  1.00 44.43  ? 197 PHE   B CD2  1 
ATOM   3324 C  CE1  . PHE   B 1 197 ? -46.076 -9.433  20.588  1.00 42.36  ? 197 PHE   B CE1  1 
ATOM   3325 C  CE2  . PHE   B 1 197 ? -43.810 -10.086 20.998  1.00 46.06  ? 197 PHE   B CE2  1 
ATOM   3326 C  CZ   . PHE   B 1 197 ? -44.973 -10.187 20.255  1.00 45.30  ? 197 PHE   B CZ   1 
ATOM   3327 N  N    . LEU   B 1 198 ? -47.634 -7.612  25.040  1.00 52.18  ? 198 LEU   B N    1 
ATOM   3328 C  CA   . LEU   B 1 198 ? -49.105 -7.693  24.935  1.00 53.92  ? 198 LEU   B CA   1 
ATOM   3329 C  C    . LEU   B 1 198 ? -49.535 -6.456  24.144  1.00 57.52  ? 198 LEU   B C    1 
ATOM   3330 O  O    . LEU   B 1 198 ? -49.400 -5.332  24.698  1.00 61.23  ? 198 LEU   B O    1 
ATOM   3331 C  CB   . LEU   B 1 198 ? -49.700 -7.752  26.348  1.00 54.33  ? 198 LEU   B CB   1 
ATOM   3332 C  CG   . LEU   B 1 198 ? -51.145 -8.235  26.468  1.00 57.37  ? 198 LEU   B CG   1 
ATOM   3333 C  CD1  . LEU   B 1 198 ? -51.523 -8.456  27.927  1.00 55.73  ? 198 LEU   B CD1  1 
ATOM   3334 C  CD2  . LEU   B 1 198 ? -52.099 -7.233  25.833  1.00 65.56  ? 198 LEU   B CD2  1 
ATOM   3335 N  N    . ILE   B 1 199 ? -49.937 -6.676  22.886  1.00 52.81  ? 199 ILE   B N    1 
ATOM   3336 C  CA   . ILE   B 1 199 ? -50.493 -5.656  21.950  1.00 53.89  ? 199 ILE   B CA   1 
ATOM   3337 C  C    . ILE   B 1 199 ? -52.022 -5.816  21.890  1.00 56.12  ? 199 ILE   B C    1 
ATOM   3338 O  O    . ILE   B 1 199 ? -52.489 -6.814  21.289  1.00 53.92  ? 199 ILE   B O    1 
ATOM   3339 C  CB   . ILE   B 1 199 ? -49.824 -5.771  20.569  1.00 48.89  ? 199 ILE   B CB   1 
ATOM   3340 C  CG1  . ILE   B 1 199 ? -48.351 -5.370  20.667  1.00 48.69  ? 199 ILE   B CG1  1 
ATOM   3341 C  CG2  . ILE   B 1 199 ? -50.571 -4.940  19.547  1.00 51.04  ? 199 ILE   B CG2  1 
ATOM   3342 C  CD1  . ILE   B 1 199 ? -47.576 -5.594  19.413  1.00 47.50  ? 199 ILE   B CD1  1 
ATOM   3343 N  N    . LYS   B 1 200 ? -52.739 -4.868  22.492  1.00 57.01  ? 200 LYS   B N    1 
ATOM   3344 C  CA   . LYS   B 1 200 ? -54.218 -4.879  22.563  1.00 60.67  ? 200 LYS   B CA   1 
ATOM   3345 C  C    . LYS   B 1 200 ? -54.774 -3.648  21.839  1.00 60.42  ? 200 LYS   B C    1 
ATOM   3346 O  O    . LYS   B 1 200 ? -54.375 -2.542  22.168  1.00 56.20  ? 200 LYS   B O    1 
ATOM   3347 C  CB   . LYS   B 1 200 ? -54.640 -4.960  24.031  1.00 65.31  ? 200 LYS   B CB   1 
ATOM   3348 C  CG   . LYS   B 1 200 ? -56.133 -4.948  24.304  1.00 73.30  ? 200 LYS   B CG   1 
ATOM   3349 C  CD   . LYS   B 1 200 ? -56.809 -6.264  24.041  1.00 90.56  ? 200 LYS   B CD   1 
ATOM   3350 C  CE   . LYS   B 1 200 ? -58.293 -6.249  24.341  1.00 95.76  ? 200 LYS   B CE   1 
ATOM   3351 N  NZ   . LYS   B 1 200 ? -58.574 -6.386  25.789  1.00 89.62  ? 200 LYS   B NZ   1 
ATOM   3352 N  N    . SER   B 1 201 ? -55.660 -3.863  20.871  1.00 59.55  ? 201 SER   B N    1 
ATOM   3353 C  CA   . SER   B 1 201 ? -56.265 -2.757  20.097  1.00 59.04  ? 201 SER   B CA   1 
ATOM   3354 C  C    . SER   B 1 201 ? -57.780 -2.792  20.263  1.00 64.45  ? 201 SER   B C    1 
ATOM   3355 O  O    . SER   B 1 201 ? -58.358 -3.850  20.102  1.00 53.14  ? 201 SER   B O    1 
ATOM   3356 C  CB   . SER   B 1 201 ? -55.881 -2.860  18.678  1.00 58.82  ? 201 SER   B CB   1 
ATOM   3357 O  OG   . SER   B 1 201 ? -56.167 -1.651  18.026  1.00 62.69  ? 201 SER   B OG   1 
ATOM   3358 N  N    . PRO   B 1 202 ? -58.440 -1.646  20.513  1.00 90.28  ? 202 PRO   B N    1 
ATOM   3359 C  CA   . PRO   B 1 202 ? -59.881 -1.599  20.756  1.00 88.46  ? 202 PRO   B CA   1 
ATOM   3360 C  C    . PRO   B 1 202 ? -60.677 -2.074  19.541  1.00 86.53  ? 202 PRO   B C    1 
ATOM   3361 O  O    . PRO   B 1 202 ? -61.693 -2.690  19.726  1.00 79.36  ? 202 PRO   B O    1 
ATOM   3362 C  CB   . PRO   B 1 202 ? -60.145 -0.122  21.037  1.00 88.37  ? 202 PRO   B CB   1 
ATOM   3363 C  CG   . PRO   B 1 202 ? -59.037 0.576   20.304  1.00 95.12  ? 202 PRO   B CG   1 
ATOM   3364 C  CD   . PRO   B 1 202 ? -57.841 -0.322  20.496  1.00 91.81  ? 202 PRO   B CD   1 
ATOM   3365 N  N    . ASP   B 1 203 ? -60.204 -1.738  18.345  1.00 88.46  ? 203 ASP   B N    1 
ATOM   3366 C  CA   . ASP   B 1 203 ? -60.887 -2.177  17.105  1.00 100.02 ? 203 ASP   B CA   1 
ATOM   3367 C  C    . ASP   B 1 203 ? -59.937 -3.041  16.274  1.00 94.12  ? 203 ASP   B C    1 
ATOM   3368 O  O    . ASP   B 1 203 ? -58.815 -3.260  16.699  1.00 87.74  ? 203 ASP   B O    1 
ATOM   3369 C  CB   . ASP   B 1 203 ? -61.486 -1.012  16.323  1.00 109.00 ? 203 ASP   B CB   1 
ATOM   3370 C  CG   . ASP   B 1 203 ? -62.861 -1.329  15.758  1.00 124.67 ? 203 ASP   B CG   1 
ATOM   3371 O  OD1  . ASP   B 1 203 ? -62.942 -1.667  14.559  1.00 133.34 ? 203 ASP   B OD1  1 
ATOM   3372 O  OD2  . ASP   B 1 203 ? -63.845 -1.230  16.522  1.00 124.47 ? 203 ASP   B OD2  1 
ATOM   3373 N  N    . SER   B 1 204 ? -60.379 -3.451  15.088  1.00 94.27  ? 204 SER   B N    1 
ATOM   3374 C  CA   . SER   B 1 204 ? -59.618 -4.348  14.181  1.00 100.61 ? 204 SER   B CA   1 
ATOM   3375 C  C    . SER   B 1 204 ? -58.392 -3.686  13.549  1.00 100.14 ? 204 SER   B C    1 
ATOM   3376 O  O    . SER   B 1 204 ? -57.675 -4.408  12.858  1.00 90.13  ? 204 SER   B O    1 
ATOM   3377 C  CB   . SER   B 1 204 ? -60.496 -4.925  13.119  1.00 110.10 ? 204 SER   B CB   1 
ATOM   3378 O  OG   . SER   B 1 204 ? -59.698 -5.432  12.061  1.00 115.41 ? 204 SER   B OG   1 
ATOM   3379 N  N    . HIS   B 1 205 ? -58.250 -2.362  13.619  1.00 101.97 ? 205 HIS   B N    1 
ATOM   3380 C  CA   . HIS   B 1 205 ? -57.028 -1.725  13.072  1.00 97.99  ? 205 HIS   B CA   1 
ATOM   3381 C  C    . HIS   B 1 205 ? -56.119 -1.269  14.216  1.00 87.20  ? 205 HIS   B C    1 
ATOM   3382 O  O    . HIS   B 1 205 ? -56.441 -0.266  14.850  1.00 80.00  ? 205 HIS   B O    1 
ATOM   3383 C  CB   . HIS   B 1 205 ? -57.400 -0.544  12.172  1.00 103.88 ? 205 HIS   B CB   1 
ATOM   3384 C  CG   . HIS   B 1 205 ? -57.559 -0.922  10.743  1.00 109.56 ? 205 HIS   B CG   1 
ATOM   3385 N  ND1  . HIS   B 1 205 ? -58.741 -0.744  10.066  1.00 112.54 ? 205 HIS   B ND1  1 
ATOM   3386 C  CD2  . HIS   B 1 205 ? -56.703 -1.485  9.870   1.00 111.99 ? 205 HIS   B CD2  1 
ATOM   3387 C  CE1  . HIS   B 1 205 ? -58.609 -1.181  8.832   1.00 105.57 ? 205 HIS   B CE1  1 
ATOM   3388 N  NE2  . HIS   B 1 205 ? -57.371 -1.639  8.687   1.00 110.64 ? 205 HIS   B NE2  1 
ATOM   3389 N  N    . PRO   B 1 206 ? -55.006 -1.971  14.504  1.00 74.78  ? 206 PRO   B N    1 
ATOM   3390 C  CA   . PRO   B 1 206 ? -54.036 -1.539  15.499  1.00 61.09  ? 206 PRO   B CA   1 
ATOM   3391 C  C    . PRO   B 1 206 ? -52.814 -0.935  14.798  1.00 51.28  ? 206 PRO   B C    1 
ATOM   3392 O  O    . PRO   B 1 206 ? -52.596 -1.283  13.685  1.00 52.92  ? 206 PRO   B O    1 
ATOM   3393 C  CB   . PRO   B 1 206 ? -53.648 -2.877  16.118  1.00 65.08  ? 206 PRO   B CB   1 
ATOM   3394 C  CG   . PRO   B 1 206 ? -53.643 -3.817  14.958  1.00 67.10  ? 206 PRO   B CG   1 
ATOM   3395 C  CD   . PRO   B 1 206 ? -54.697 -3.300  14.008  1.00 68.03  ? 206 PRO   B CD   1 
ATOM   3396 N  N    . ALA   B 1 207 ? -52.096 -0.038  15.478  1.00 46.45  ? 207 ALA   B N    1 
ATOM   3397 C  CA   . ALA   B 1 207 ? -50.870 0.626   14.977  1.00 43.84  ? 207 ALA   B CA   1 
ATOM   3398 C  C    . ALA   B 1 207 ? -50.067 1.150   16.168  1.00 45.17  ? 207 ALA   B C    1 
ATOM   3399 O  O    . ALA   B 1 207 ? -50.682 1.397   17.180  1.00 39.57  ? 207 ALA   B O    1 
ATOM   3400 C  CB   . ALA   B 1 207 ? -51.250 1.746   14.059  1.00 45.69  ? 207 ALA   B CB   1 
ATOM   3401 N  N    . ASP   B 1 208 ? -48.744 1.296   16.063  1.00 43.95  ? 208 ASP   B N    1 
ATOM   3402 C  CA   . ASP   B 1 208 ? -47.933 1.078   14.862  1.00 46.58  ? 208 ASP   B CA   1 
ATOM   3403 C  C    . ASP   B 1 208 ? -46.942 -0.102  15.054  1.00 47.14  ? 208 ASP   B C    1 
ATOM   3404 O  O    . ASP   B 1 208 ? -46.464 -0.702  14.042  1.00 50.80  ? 208 ASP   B O    1 
ATOM   3405 C  CB   . ASP   B 1 208 ? -47.219 2.382   14.460  1.00 48.77  ? 208 ASP   B CB   1 
ATOM   3406 C  CG   . ASP   B 1 208 ? -48.047 3.293   13.557  1.00 55.89  ? 208 ASP   B CG   1 
ATOM   3407 O  OD1  . ASP   B 1 208 ? -48.889 4.060   14.098  1.00 51.94  ? 208 ASP   B OD1  1 
ATOM   3408 O  OD2  . ASP   B 1 208 ? -47.852 3.225   12.297  1.00 51.87  ? 208 ASP   B OD2  1 
ATOM   3409 N  N    . GLY   B 1 209 ? -46.591 -0.415  16.299  1.00 45.96  ? 209 GLY   B N    1 
ATOM   3410 C  CA   . GLY   B 1 209 ? -45.790 -1.595  16.664  1.00 52.29  ? 209 GLY   B CA   1 
ATOM   3411 C  C    . GLY   B 1 209 ? -44.702 -1.317  17.700  1.00 49.47  ? 209 GLY   B C    1 
ATOM   3412 O  O    . GLY   B 1 209 ? -44.654 -0.224  18.317  1.00 48.42  ? 209 GLY   B O    1 
ATOM   3413 N  N    . ILE   B 1 210 ? -43.855 -2.323  17.871  1.00 46.10  ? 210 ILE   B N    1 
ATOM   3414 C  CA   . ILE   B 1 210 ? -42.739 -2.383  18.853  1.00 43.20  ? 210 ILE   B CA   1 
ATOM   3415 C  C    . ILE   B 1 210 ? -41.489 -2.749  18.077  1.00 39.07  ? 210 ILE   B C    1 
ATOM   3416 O  O    . ILE   B 1 210 ? -41.596 -3.426  17.062  1.00 37.87  ? 210 ILE   B O    1 
ATOM   3417 C  CB   . ILE   B 1 210 ? -43.047 -3.386  19.969  1.00 45.98  ? 210 ILE   B CB   1 
ATOM   3418 C  CG1  . ILE   B 1 210 ? -44.407 -3.073  20.605  1.00 47.07  ? 210 ILE   B CG1  1 
ATOM   3419 C  CG2  . ILE   B 1 210 ? -41.907 -3.387  20.976  1.00 50.56  ? 210 ILE   B CG2  1 
ATOM   3420 C  CD1  . ILE   B 1 210 ? -44.869 -4.101  21.606  1.00 54.47  ? 210 ILE   B CD1  1 
ATOM   3421 N  N    . ALA   B 1 211 ? -40.375 -2.173  18.478  1.00 39.31  ? 211 ALA   B N    1 
ATOM   3422 C  CA   . ALA   B 1 211 ? -39.044 -2.544  17.985  1.00 43.12  ? 211 ALA   B CA   1 
ATOM   3423 C  C    . ALA   B 1 211 ? -38.131 -2.745  19.183  1.00 42.79  ? 211 ALA   B C    1 
ATOM   3424 O  O    . ALA   B 1 211 ? -38.283 -2.026  20.213  1.00 44.81  ? 211 ALA   B O    1 
ATOM   3425 C  CB   . ALA   B 1 211 ? -38.509 -1.500  17.049  1.00 48.05  ? 211 ALA   B CB   1 
ATOM   3426 N  N    . PHE   B 1 212 ? -37.271 -3.752  19.066  1.00 41.29  ? 212 PHE   B N    1 
ATOM   3427 C  CA   . PHE   B 1 212 ? -35.999 -3.849  19.804  1.00 41.37  ? 212 PHE   B CA   1 
ATOM   3428 C  C    . PHE   B 1 212 ? -34.950 -3.137  18.955  1.00 41.74  ? 212 PHE   B C    1 
ATOM   3429 O  O    . PHE   B 1 212 ? -34.934 -3.396  17.740  1.00 44.90  ? 212 PHE   B O    1 
ATOM   3430 C  CB   . PHE   B 1 212 ? -35.603 -5.298  20.051  1.00 43.61  ? 212 PHE   B CB   1 
ATOM   3431 C  CG   . PHE   B 1 212 ? -34.160 -5.409  20.470  1.00 45.75  ? 212 PHE   B CG   1 
ATOM   3432 C  CD1  . PHE   B 1 212 ? -33.796 -5.202  21.786  1.00 45.19  ? 212 PHE   B CD1  1 
ATOM   3433 C  CD2  . PHE   B 1 212 ? -33.172 -5.665  19.546  1.00 46.59  ? 212 PHE   B CD2  1 
ATOM   3434 C  CE1  . PHE   B 1 212 ? -32.475 -5.291  22.173  1.00 45.09  ? 212 PHE   B CE1  1 
ATOM   3435 C  CE2  . PHE   B 1 212 ? -31.845 -5.749  19.934  1.00 49.61  ? 212 PHE   B CE2  1 
ATOM   3436 C  CZ   . PHE   B 1 212 ? -31.502 -5.575  21.248  1.00 47.89  ? 212 PHE   B CZ   1 
ATOM   3437 N  N    . PHE   B 1 213 ? -34.133 -2.253  19.543  1.00 40.39  ? 213 PHE   B N    1 
ATOM   3438 C  CA   . PHE   B 1 213 ? -33.108 -1.505  18.777  1.00 42.07  ? 213 PHE   B CA   1 
ATOM   3439 C  C    . PHE   B 1 213 ? -31.800 -1.374  19.561  1.00 46.96  ? 213 PHE   B C    1 
ATOM   3440 O  O    . PHE   B 1 213 ? -31.742 -1.525  20.820  1.00 42.61  ? 213 PHE   B O    1 
ATOM   3441 C  CB   . PHE   B 1 213 ? -33.635 -0.129  18.378  1.00 44.18  ? 213 PHE   B CB   1 
ATOM   3442 C  CG   . PHE   B 1 213 ? -33.799 0.818   19.540  1.00 41.55  ? 213 PHE   B CG   1 
ATOM   3443 C  CD1  . PHE   B 1 213 ? -34.947 0.793   20.320  1.00 43.85  ? 213 PHE   B CD1  1 
ATOM   3444 C  CD2  . PHE   B 1 213 ? -32.801 1.727   19.849  1.00 41.30  ? 213 PHE   B CD2  1 
ATOM   3445 C  CE1  . PHE   B 1 213 ? -35.102 1.670   21.384  1.00 46.31  ? 213 PHE   B CE1  1 
ATOM   3446 C  CE2  . PHE   B 1 213 ? -32.952 2.608   20.912  1.00 48.23  ? 213 PHE   B CE2  1 
ATOM   3447 C  CZ   . PHE   B 1 213 ? -34.100 2.578   21.682  1.00 46.50  ? 213 PHE   B CZ   1 
ATOM   3448 N  N    . ILE   B 1 214 ? -30.765 -1.093  18.772  1.00 47.37  ? 214 ILE   B N    1 
ATOM   3449 C  CA   . ILE   B 1 214 ? -29.356 -0.850  19.176  1.00 45.80  ? 214 ILE   B CA   1 
ATOM   3450 C  C    . ILE   B 1 214 ? -29.003 0.463   18.505  1.00 47.34  ? 214 ILE   B C    1 
ATOM   3451 O  O    . ILE   B 1 214 ? -29.197 0.548   17.278  1.00 49.24  ? 214 ILE   B O    1 
ATOM   3452 C  CB   . ILE   B 1 214 ? -28.423 -1.988  18.709  1.00 45.92  ? 214 ILE   B CB   1 
ATOM   3453 C  CG1  . ILE   B 1 214 ? -28.940 -3.360  19.150  1.00 52.18  ? 214 ILE   B CG1  1 
ATOM   3454 C  CG2  . ILE   B 1 214 ? -27.009 -1.746  19.197  1.00 48.57  ? 214 ILE   B CG2  1 
ATOM   3455 C  CD1  . ILE   B 1 214 ? -28.140 -4.534  18.640  1.00 56.09  ? 214 ILE   B CD1  1 
ATOM   3456 N  N    . SER   B 1 215 ? -28.538 1.432   19.282  1.00 50.62  ? 215 SER   B N    1 
ATOM   3457 C  CA   . SER   B 1 215 ? -28.239 2.820   18.850  1.00 52.50  ? 215 SER   B CA   1 
ATOM   3458 C  C    . SER   B 1 215 ? -26.936 3.317   19.482  1.00 54.82  ? 215 SER   B C    1 
ATOM   3459 O  O    . SER   B 1 215 ? -26.411 2.664   20.420  1.00 57.48  ? 215 SER   B O    1 
ATOM   3460 C  CB   . SER   B 1 215 ? -29.357 3.725   19.248  1.00 56.29  ? 215 SER   B CB   1 
ATOM   3461 O  OG   . SER   B 1 215 ? -29.351 3.877   20.666  1.00 62.31  ? 215 SER   B OG   1 
ATOM   3462 N  N    . ASN   B 1 216 ? -26.461 4.464   19.010  1.00 54.72  ? 216 ASN   B N    1 
ATOM   3463 C  CA   . ASN   B 1 216 ? -25.415 5.274   19.682  1.00 55.58  ? 216 ASN   B CA   1 
ATOM   3464 C  C    . ASN   B 1 216 ? -25.915 5.593   21.100  1.00 53.70  ? 216 ASN   B C    1 
ATOM   3465 O  O    . ASN   B 1 216 ? -27.138 5.584   21.322  1.00 52.34  ? 216 ASN   B O    1 
ATOM   3466 C  CB   . ASN   B 1 216 ? -25.037 6.501   18.843  1.00 61.60  ? 216 ASN   B CB   1 
ATOM   3467 C  CG   . ASN   B 1 216 ? -26.234 7.386   18.558  1.00 69.87  ? 216 ASN   B CG   1 
ATOM   3468 O  OD1  . ASN   B 1 216 ? -27.039 7.078   17.678  1.00 73.21  ? 216 ASN   B OD1  1 
ATOM   3469 N  ND2  . ASN   B 1 216 ? -26.377 8.463   19.317  1.00 68.23  ? 216 ASN   B ND2  1 
ATOM   3470 N  N    . ILE   B 1 217 ? -24.982 5.790   22.035  1.00 55.76  ? 217 ILE   B N    1 
ATOM   3471 C  CA   . ILE   B 1 217 ? -25.239 5.822   23.500  1.00 57.65  ? 217 ILE   B CA   1 
ATOM   3472 C  C    . ILE   B 1 217 ? -26.219 6.969   23.821  1.00 58.84  ? 217 ILE   B C    1 
ATOM   3473 O  O    . ILE   B 1 217 ? -27.112 6.768   24.687  1.00 51.36  ? 217 ILE   B O    1 
ATOM   3474 C  CB   . ILE   B 1 217 ? -23.907 5.896   24.293  1.00 64.07  ? 217 ILE   B CB   1 
ATOM   3475 C  CG1  . ILE   B 1 217 ? -23.083 7.142   23.948  1.00 78.99  ? 217 ILE   B CG1  1 
ATOM   3476 C  CG2  . ILE   B 1 217 ? -23.086 4.620   24.117  1.00 55.66  ? 217 ILE   B CG2  1 
ATOM   3477 C  CD1  . ILE   B 1 217 ? -21.672 7.150   24.536  1.00 86.43  ? 217 ILE   B CD1  1 
ATOM   3478 N  N    . ASP   B 1 218 ? -26.079 8.125   23.160  1.00 51.87  ? 218 ASP   B N    1 
ATOM   3479 C  CA   . ASP   B 1 218 ? -26.897 9.339   23.449  1.00 57.49  ? 218 ASP   B CA   1 
ATOM   3480 C  C    . ASP   B 1 218 ? -28.140 9.389   22.536  1.00 57.74  ? 218 ASP   B C    1 
ATOM   3481 O  O    . ASP   B 1 218 ? -28.816 10.425  22.528  1.00 61.09  ? 218 ASP   B O    1 
ATOM   3482 C  CB   . ASP   B 1 218 ? -26.053 10.621  23.389  1.00 64.37  ? 218 ASP   B CB   1 
ATOM   3483 C  CG   . ASP   B 1 218 ? -25.501 10.988  22.017  1.00 78.42  ? 218 ASP   B CG   1 
ATOM   3484 O  OD1  . ASP   B 1 218 ? -25.434 10.089  21.142  1.00 93.53  ? 218 ASP   B OD1  1 
ATOM   3485 O  OD2  . ASP   B 1 218 ? -25.117 12.170  21.834  1.00 76.76  ? 218 ASP   B OD2  1 
ATOM   3486 N  N    . SER   B 1 219 ? -28.488 8.292   21.858  1.00 53.55  ? 219 SER   B N    1 
ATOM   3487 C  CA   . SER   B 1 219 ? -29.729 8.157   21.058  1.00 57.26  ? 219 SER   B CA   1 
ATOM   3488 C  C    . SER   B 1 219 ? -30.916 8.671   21.857  1.00 55.95  ? 219 SER   B C    1 
ATOM   3489 O  O    . SER   B 1 219 ? -31.004 8.344   23.064  1.00 55.10  ? 219 SER   B O    1 
ATOM   3490 C  CB   . SER   B 1 219 ? -29.990 6.742   20.617  1.00 60.91  ? 219 SER   B CB   1 
ATOM   3491 O  OG   . SER   B 1 219 ? -31.183 6.660   19.851  1.00 53.81  ? 219 SER   B OG   1 
ATOM   3492 N  N    . SER   B 1 220 ? -31.790 9.418   21.174  1.00 55.50  ? 220 SER   B N    1 
ATOM   3493 C  CA   . SER   B 1 220 ? -33.062 9.950   21.725  1.00 58.08  ? 220 SER   B CA   1 
ATOM   3494 C  C    . SER   B 1 220 ? -34.112 9.993   20.615  1.00 48.11  ? 220 SER   B C    1 
ATOM   3495 O  O    . SER   B 1 220 ? -33.765 9.741   19.435  1.00 49.66  ? 220 SER   B O    1 
ATOM   3496 C  CB   . SER   B 1 220 ? -32.869 11.299  22.335  1.00 62.26  ? 220 SER   B CB   1 
ATOM   3497 O  OG   . SER   B 1 220 ? -32.519 12.208  21.313  1.00 59.23  ? 220 SER   B OG   1 
ATOM   3498 N  N    . ILE   B 1 221 ? -35.367 10.214  21.008  1.00 50.86  ? 221 ILE   B N    1 
ATOM   3499 C  CA   . ILE   B 1 221 ? -36.561 10.091  20.120  1.00 50.79  ? 221 ILE   B CA   1 
ATOM   3500 C  C    . ILE   B 1 221 ? -36.443 11.193  19.082  1.00 52.90  ? 221 ILE   B C    1 
ATOM   3501 O  O    . ILE   B 1 221 ? -36.484 12.359  19.443  1.00 53.71  ? 221 ILE   B O    1 
ATOM   3502 C  CB   . ILE   B 1 221 ? -37.887 10.211  20.900  1.00 49.58  ? 221 ILE   B CB   1 
ATOM   3503 C  CG1  . ILE   B 1 221 ? -38.127 9.028   21.839  1.00 49.98  ? 221 ILE   B CG1  1 
ATOM   3504 C  CG2  . ILE   B 1 221 ? -39.053 10.372  19.938  1.00 53.75  ? 221 ILE   B CG2  1 
ATOM   3505 C  CD1  . ILE   B 1 221 ? -39.316 9.217   22.762  1.00 50.89  ? 221 ILE   B CD1  1 
ATOM   3506 N  N    . PRO   B 1 222 ? -36.275 10.875  17.782  1.00 54.63  ? 222 PRO   B N    1 
ATOM   3507 C  CA   . PRO   B 1 222 ? -36.182 11.920  16.767  1.00 52.49  ? 222 PRO   B CA   1 
ATOM   3508 C  C    . PRO   B 1 222 ? -37.529 12.649  16.661  1.00 55.71  ? 222 PRO   B C    1 
ATOM   3509 O  O    . PRO   B 1 222 ? -38.529 12.035  16.946  1.00 57.96  ? 222 PRO   B O    1 
ATOM   3510 C  CB   . PRO   B 1 222 ? -35.810 11.204  15.459  1.00 48.10  ? 222 PRO   B CB   1 
ATOM   3511 C  CG   . PRO   B 1 222 ? -35.736 9.713   15.797  1.00 49.88  ? 222 PRO   B CG   1 
ATOM   3512 C  CD   . PRO   B 1 222 ? -36.216 9.518   17.228  1.00 50.60  ? 222 PRO   B CD   1 
ATOM   3513 N  N    . SER   B 1 223 ? -37.515 13.926  16.255  1.00 65.41  ? 223 SER   B N    1 
ATOM   3514 C  CA   . SER   B 1 223 ? -38.719 14.773  16.021  1.00 64.51  ? 223 SER   B CA   1 
ATOM   3515 C  C    . SER   B 1 223 ? -39.644 14.134  14.987  1.00 62.18  ? 223 SER   B C    1 
ATOM   3516 O  O    . SER   B 1 223 ? -39.131 13.696  13.913  1.00 62.85  ? 223 SER   B O    1 
ATOM   3517 C  CB   . SER   B 1 223 ? -38.335 16.154  15.580  1.00 64.44  ? 223 SER   B CB   1 
ATOM   3518 O  OG   . SER   B 1 223 ? -38.096 16.962  16.716  1.00 69.69  ? 223 SER   B OG   1 
ATOM   3519 N  N    . GLY   B 1 224 ? -40.943 14.112  15.300  1.00 58.33  ? 224 GLY   B N    1 
ATOM   3520 C  CA   . GLY   B 1 224 ? -42.026 13.743  14.361  1.00 64.86  ? 224 GLY   B CA   1 
ATOM   3521 C  C    . GLY   B 1 224 ? -42.030 12.266  14.008  1.00 64.67  ? 224 GLY   B C    1 
ATOM   3522 O  O    . GLY   B 1 224 ? -42.465 11.939  12.889  1.00 65.31  ? 224 GLY   B O    1 
ATOM   3523 N  N    . SER   B 1 225 ? -41.586 11.415  14.947  1.00 63.22  ? 225 SER   B N    1 
ATOM   3524 C  CA   . SER   B 1 225 ? -41.330 9.958   14.779  1.00 57.52  ? 225 SER   B CA   1 
ATOM   3525 C  C    . SER   B 1 225 ? -42.450 9.121   15.390  1.00 46.41  ? 225 SER   B C    1 
ATOM   3526 O  O    . SER   B 1 225 ? -42.201 7.951   15.659  1.00 55.14  ? 225 SER   B O    1 
ATOM   3527 C  CB   . SER   B 1 225 ? -39.997 9.557   15.386  1.00 59.03  ? 225 SER   B CB   1 
ATOM   3528 O  OG   . SER   B 1 225 ? -40.057 9.532   16.804  1.00 48.77  ? 225 SER   B OG   1 
ATOM   3529 N  N    . THR   B 1 226 ? -43.624 9.694   15.615  1.00 43.99  ? 226 THR   B N    1 
ATOM   3530 C  CA   . THR   B 1 226 ? -44.837 8.947   16.021  1.00 50.54  ? 226 THR   B CA   1 
ATOM   3531 C  C    . THR   B 1 226 ? -45.277 8.089   14.829  1.00 47.39  ? 226 THR   B C    1 
ATOM   3532 O  O    . THR   B 1 226 ? -44.683 8.229   13.749  1.00 51.32  ? 226 THR   B O    1 
ATOM   3533 C  CB   . THR   B 1 226 ? -45.917 9.906   16.532  1.00 52.00  ? 226 THR   B CB   1 
ATOM   3534 O  OG1  . THR   B 1 226 ? -45.984 10.905  15.516  1.00 59.46  ? 226 THR   B OG1  1 
ATOM   3535 C  CG2  . THR   B 1 226 ? -45.582 10.551  17.855  1.00 49.01  ? 226 THR   B CG2  1 
ATOM   3536 N  N    . GLY   B 1 227 ? -46.284 7.243   15.033  1.00 48.47  ? 227 GLY   B N    1 
ATOM   3537 C  CA   . GLY   B 1 227 ? -46.827 6.332   14.010  1.00 50.61  ? 227 GLY   B CA   1 
ATOM   3538 C  C    . GLY   B 1 227 ? -45.725 5.520   13.346  1.00 54.90  ? 227 GLY   B C    1 
ATOM   3539 O  O    . GLY   B 1 227 ? -44.967 4.795   14.048  1.00 54.26  ? 227 GLY   B O    1 
ATOM   3540 N  N    . ARG   B 1 228 ? -45.600 5.660   12.031  1.00 56.33  ? 228 ARG   B N    1 
ATOM   3541 C  CA   . ARG   B 1 228 ? -44.926 4.663   11.148  1.00 54.37  ? 228 ARG   B CA   1 
ATOM   3542 C  C    . ARG   B 1 228 ? -43.413 4.601   11.366  1.00 43.04  ? 228 ARG   B C    1 
ATOM   3543 O  O    . ARG   B 1 228 ? -42.814 3.682   10.810  1.00 43.77  ? 228 ARG   B O    1 
ATOM   3544 C  CB   . ARG   B 1 228 ? -45.189 4.993   9.676   1.00 52.90  ? 228 ARG   B CB   1 
ATOM   3545 C  CG   . ARG   B 1 228 ? -44.746 6.393   9.288   1.00 52.55  ? 228 ARG   B CG   1 
ATOM   3546 C  CD   . ARG   B 1 228 ? -45.222 6.652   7.894   1.00 55.99  ? 228 ARG   B CD   1 
ATOM   3547 N  NE   . ARG   B 1 228 ? -44.641 7.832   7.282   1.00 57.55  ? 228 ARG   B NE   1 
ATOM   3548 C  CZ   . ARG   B 1 228 ? -44.835 8.152   6.011   1.00 56.65  ? 228 ARG   B CZ   1 
ATOM   3549 N  NH1  . ARG   B 1 228 ? -45.590 7.390   5.238   1.00 61.88  ? 228 ARG   B NH1  1 
ATOM   3550 N  NH2  . ARG   B 1 228 ? -44.282 9.229   5.513   1.00 60.99  ? 228 ARG   B NH2  1 
ATOM   3551 N  N    . LEU   B 1 229 ? -42.822 5.588   12.040  1.00 44.80  ? 229 LEU   B N    1 
ATOM   3552 C  CA   . LEU   B 1 229 ? -41.354 5.725   12.234  1.00 44.65  ? 229 LEU   B CA   1 
ATOM   3553 C  C    . LEU   B 1 229 ? -40.942 5.136   13.591  1.00 49.19  ? 229 LEU   B C    1 
ATOM   3554 O  O    . LEU   B 1 229 ? -39.727 5.192   13.935  1.00 48.25  ? 229 LEU   B O    1 
ATOM   3555 C  CB   . LEU   B 1 229 ? -41.007 7.211   12.143  1.00 49.01  ? 229 LEU   B CB   1 
ATOM   3556 C  CG   . LEU   B 1 229 ? -41.264 7.859   10.779  1.00 53.37  ? 229 LEU   B CG   1 
ATOM   3557 C  CD1  . LEU   B 1 229 ? -40.659 9.249   10.725  1.00 56.65  ? 229 LEU   B CD1  1 
ATOM   3558 C  CD2  . LEU   B 1 229 ? -40.719 7.013   9.634   1.00 55.77  ? 229 LEU   B CD2  1 
ATOM   3559 N  N    . LEU   B 1 230 ? -41.928 4.651   14.353  1.00 46.44  ? 230 LEU   B N    1 
ATOM   3560 C  CA   . LEU   B 1 230 ? -41.752 3.725   15.496  1.00 48.79  ? 230 LEU   B CA   1 
ATOM   3561 C  C    . LEU   B 1 230 ? -40.859 4.314   16.609  1.00 52.53  ? 230 LEU   B C    1 
ATOM   3562 O  O    . LEU   B 1 230 ? -40.420 3.516   17.430  1.00 51.86  ? 230 LEU   B O    1 
ATOM   3563 C  CB   . LEU   B 1 230 ? -41.143 2.430   14.949  1.00 51.91  ? 230 LEU   B CB   1 
ATOM   3564 C  CG   . LEU   B 1 230 ? -41.997 1.613   13.973  1.00 55.03  ? 230 LEU   B CG   1 
ATOM   3565 C  CD1  . LEU   B 1 230 ? -41.204 0.426   13.449  1.00 63.39  ? 230 LEU   B CD1  1 
ATOM   3566 C  CD2  . LEU   B 1 230 ? -43.288 1.132   14.623  1.00 52.30  ? 230 LEU   B CD2  1 
ATOM   3567 N  N    . GLY   B 1 231 ? -40.607 5.633   16.674  1.00 45.49  ? 231 GLY   B N    1 
ATOM   3568 C  CA   . GLY   B 1 231 ? -39.687 6.237   17.667  1.00 45.94  ? 231 GLY   B CA   1 
ATOM   3569 C  C    . GLY   B 1 231 ? -38.208 6.095   17.307  1.00 48.02  ? 231 GLY   B C    1 
ATOM   3570 O  O    . GLY   B 1 231 ? -37.345 6.514   18.116  1.00 47.32  ? 231 GLY   B O    1 
ATOM   3571 N  N    . LEU   B 1 232 ? -37.899 5.574   16.122  1.00 45.69  ? 232 LEU   B N    1 
ATOM   3572 C  CA   . LEU   B 1 232 ? -36.523 5.169   15.758  1.00 50.57  ? 232 LEU   B CA   1 
ATOM   3573 C  C    . LEU   B 1 232 ? -35.878 6.141   14.765  1.00 53.61  ? 232 LEU   B C    1 
ATOM   3574 O  O    . LEU   B 1 232 ? -34.658 6.361   14.917  1.00 54.64  ? 232 LEU   B O    1 
ATOM   3575 C  CB   . LEU   B 1 232 ? -36.587 3.762   15.158  1.00 55.55  ? 232 LEU   B CB   1 
ATOM   3576 C  CG   . LEU   B 1 232 ? -37.036 2.633   16.088  1.00 47.97  ? 232 LEU   B CG   1 
ATOM   3577 C  CD1  . LEU   B 1 232 ? -36.836 1.295   15.403  1.00 47.73  ? 232 LEU   B CD1  1 
ATOM   3578 C  CD2  . LEU   B 1 232 ? -36.275 2.643   17.391  1.00 50.08  ? 232 LEU   B CD2  1 
ATOM   3579 N  N    . PHE   B 1 233 ? -36.643 6.679   13.790  1.00 60.40  ? 233 PHE   B N    1 
ATOM   3580 C  CA   . PHE   B 1 233 ? -36.135 7.451   12.611  1.00 59.09  ? 233 PHE   B CA   1 
ATOM   3581 C  C    . PHE   B 1 233 ? -36.751 8.850   12.471  1.00 58.28  ? 233 PHE   B C    1 
ATOM   3582 O  O    . PHE   B 1 233 ? -37.930 9.078   12.772  1.00 52.16  ? 233 PHE   B O    1 
ATOM   3583 C  CB   . PHE   B 1 233 ? -36.369 6.653   11.327  1.00 58.83  ? 233 PHE   B CB   1 
ATOM   3584 C  CG   . PHE   B 1 233 ? -35.704 5.302   11.345  1.00 58.46  ? 233 PHE   B CG   1 
ATOM   3585 C  CD1  . PHE   B 1 233 ? -34.355 5.187   11.065  1.00 56.37  ? 233 PHE   B CD1  1 
ATOM   3586 C  CD2  . PHE   B 1 233 ? -36.426 4.160   11.655  1.00 53.98  ? 233 PHE   B CD2  1 
ATOM   3587 C  CE1  . PHE   B 1 233 ? -33.743 3.946   11.088  1.00 63.82  ? 233 PHE   B CE1  1 
ATOM   3588 C  CE2  . PHE   B 1 233 ? -35.806 2.927   11.693  1.00 54.19  ? 233 PHE   B CE2  1 
ATOM   3589 C  CZ   . PHE   B 1 233 ? -34.469 2.820   11.408  1.00 56.82  ? 233 PHE   B CZ   1 
ATOM   3590 N  N    . PRO   B 1 234 ? -35.964 9.837   11.967  1.00 61.37  ? 234 PRO   B N    1 
ATOM   3591 C  CA   . PRO   B 1 234 ? -36.469 11.197  11.752  1.00 61.52  ? 234 PRO   B CA   1 
ATOM   3592 C  C    . PRO   B 1 234 ? -37.360 11.294  10.504  1.00 66.64  ? 234 PRO   B C    1 
ATOM   3593 O  O    . PRO   B 1 234 ? -38.227 12.141  10.484  1.00 67.87  ? 234 PRO   B O    1 
ATOM   3594 C  CB   . PRO   B 1 234 ? -35.185 12.011  11.562  1.00 55.41  ? 234 PRO   B CB   1 
ATOM   3595 C  CG   . PRO   B 1 234 ? -34.233 11.030  10.904  1.00 56.18  ? 234 PRO   B CG   1 
ATOM   3596 C  CD   . PRO   B 1 234 ? -34.557 9.692   11.541  1.00 58.28  ? 234 PRO   B CD   1 
ATOM   3597 N  N    . ASP   B 1 235 ? -37.128 10.412  9.521   1.00 65.44  ? 235 ASP   B N    1 
ATOM   3598 C  CA   . ASP   B 1 235 ? -37.791 10.411  8.190   1.00 66.84  ? 235 ASP   B CA   1 
ATOM   3599 C  C    . ASP   B 1 235 ? -37.900 8.970   7.696   1.00 61.45  ? 235 ASP   B C    1 
ATOM   3600 O  O    . ASP   B 1 235 ? -37.279 8.092   8.335   1.00 65.48  ? 235 ASP   B O    1 
ATOM   3601 C  CB   . ASP   B 1 235 ? -36.993 11.220  7.165   1.00 64.94  ? 235 ASP   B CB   1 
ATOM   3602 C  CG   . ASP   B 1 235 ? -35.612 10.623  6.924   1.00 75.89  ? 235 ASP   B CG   1 
ATOM   3603 O  OD1  . ASP   B 1 235 ? -35.538 9.507   6.318   1.00 68.66  ? 235 ASP   B OD1  1 
ATOM   3604 O  OD2  . ASP   B 1 235 ? -34.619 11.253  7.379   1.00 69.60  ? 235 ASP   B OD2  1 
ATOM   3605 N  N    . ALA   B 1 236 ? -38.607 8.764   6.576   1.00 55.66  ? 236 ALA   B N    1 
ATOM   3606 C  CA   . ALA   B 1 236 ? -38.876 7.437   5.977   1.00 57.46  ? 236 ALA   B CA   1 
ATOM   3607 C  C    . ALA   B 1 236 ? -37.948 7.174   4.768   1.00 60.45  ? 236 ALA   B C    1 
ATOM   3608 O  O    . ALA   B 1 236 ? -38.205 6.205   4.047   1.00 63.85  ? 236 ALA   B O    1 
ATOM   3609 C  CB   . ALA   B 1 236 ? -40.347 7.307   5.646   1.00 55.72  ? 236 ALA   B CB   1 
ATOM   3610 N  N    . ASN   B 1 237 ? -36.836 7.903   4.610   1.00 61.13  ? 237 ASN   B N    1 
ATOM   3611 C  CA   . ASN   B 1 237 ? -35.790 7.547   3.609   1.00 75.05  ? 237 ASN   B CA   1 
ATOM   3612 C  C    . ASN   B 1 237 ? -35.189 6.184   3.987   1.00 81.87  ? 237 ASN   B C    1 
ATOM   3613 O  O    . ASN   B 1 237 ? -34.924 5.881   5.162   1.00 78.69  ? 237 ASN   B O    1 
ATOM   3614 C  CB   . ASN   B 1 237 ? -34.713 8.633   3.461   1.00 81.08  ? 237 ASN   B CB   1 
ATOM   3615 C  CG   . ASN   B 1 237 ? -35.265 9.944   2.932   1.00 79.06  ? 237 ASN   B CG   1 
ATOM   3616 O  OD1  . ASN   B 1 237 ? -36.293 9.964   2.254   1.00 73.00  ? 237 ASN   B OD1  1 
ATOM   3617 N  ND2  . ASN   B 1 237 ? -34.597 11.041  3.245   1.00 69.97  ? 237 ASN   B ND2  1 
ATOM   3618 O  OXT  . ASN   B 1 237 ? -34.959 5.339   3.114   1.00 86.97  ? 237 ASN   B OXT  1 
HETATM 3619 MN MN   . MN    C 2 .   ? -10.142 -33.845 7.086   1.00 41.47  ? 301 MN    A MN   1 
HETATM 3620 CA CA   . CA    D 3 .   ? -6.848  -36.126 7.931   1.00 40.18  ? 302 CA    A CA   1 
HETATM 3621 C  C12  . A1EAT E 4 .   ? -54.622 10.412  5.619   1.00 45.75  ? 301 A1EAT B C12  1 
HETATM 3622 C  C14  . A1EAT E 4 .   ? -53.698 12.647  5.063   1.00 44.15  ? 301 A1EAT B C14  1 
HETATM 3623 C  C15  . A1EAT E 4 .   ? -58.171 15.627  -3.405  1.00 40.79  ? 301 A1EAT B C15  1 
HETATM 3624 C  C9   . A1EAT E 4 .   ? -54.808 12.998  4.259   1.00 48.52  ? 301 A1EAT B C9   1 
HETATM 3625 C  C10  . A1EAT E 4 .   ? -55.781 11.951  4.190   1.00 42.25  ? 301 A1EAT B C10  1 
HETATM 3626 C  C11  . A1EAT E 4 .   ? -55.695 10.693  4.796   1.00 37.65  ? 301 A1EAT B C11  1 
HETATM 3627 C  C13  . A1EAT E 4 .   ? -53.627 11.408  5.753   1.00 42.96  ? 301 A1EAT B C13  1 
HETATM 3628 O  O7   . A1EAT E 4 .   ? -55.582 8.549   6.753   1.00 43.47  ? 301 A1EAT B O7   1 
HETATM 3629 C  C24  . A1EAT E 4 .   ? -54.548 9.074   6.345   1.00 44.59  ? 301 A1EAT B C24  1 
HETATM 3630 C  CG   . A1EAT E 4 .   ? -54.701 15.537  3.941   1.00 47.54  ? 301 A1EAT B CG   1 
HETATM 3631 C  CD2  . A1EAT E 4 .   ? -55.178 16.322  2.818   1.00 48.78  ? 301 A1EAT B CD2  1 
HETATM 3632 N  NE2  . A1EAT E 4 .   ? -55.685 15.382  1.893   1.00 54.16  ? 301 A1EAT B NE2  1 
HETATM 3633 C  CE1  . A1EAT E 4 .   ? -55.595 14.109  2.377   1.00 48.80  ? 301 A1EAT B CE1  1 
HETATM 3634 N  ND1  . A1EAT E 4 .   ? -54.988 14.203  3.585   1.00 54.57  ? 301 A1EAT B ND1  1 
HETATM 3635 C  C    . A1EAT E 4 .   ? -57.468 15.555  -2.093  1.00 45.36  ? 301 A1EAT B C    1 
HETATM 3636 C  C1   . A1EAT E 4 .   ? -57.204 14.374  -1.475  1.00 44.32  ? 301 A1EAT B C1   1 
HETATM 3637 C  C2   . A1EAT E 4 .   ? -56.590 14.376  -0.193  1.00 50.54  ? 301 A1EAT B C2   1 
HETATM 3638 C  C3   . A1EAT E 4 .   ? -56.259 15.506  0.624   1.00 49.85  ? 301 A1EAT B C3   1 
HETATM 3639 C  C4   . A1EAT E 4 .   ? -56.630 16.678  -0.046  1.00 51.99  ? 301 A1EAT B C4   1 
HETATM 3640 C  C5   . A1EAT E 4 .   ? -57.187 16.714  -1.351  1.00 53.10  ? 301 A1EAT B C5   1 
HETATM 3641 O  O    . A1EAT E 4 .   ? -58.509 16.710  -3.794  1.00 45.18  ? 301 A1EAT B O    1 
HETATM 3642 C  C16  . A1EAT E 4 .   ? -59.241 14.700  -5.344  1.00 39.36  ? 301 A1EAT B C16  1 
HETATM 3643 N  N2   . A1EAT E 4 .   ? -58.508 14.577  -4.110  1.00 42.03  ? 301 A1EAT B N2   1 
HETATM 3644 C  C23  . A1EAT E 4 .   ? -59.054 13.539  -6.311  1.00 40.84  ? 301 A1EAT B C23  1 
HETATM 3645 O  O1M  . A1EAT E 4 .   ? -57.678 13.441  -6.760  1.00 38.26  ? 301 A1EAT B O1M  1 
HETATM 3646 C  C1M  . A1EAT E 4 .   ? -57.540 12.973  -8.099  1.00 38.91  ? 301 A1EAT B C1M  1 
HETATM 3647 C  C2M  . A1EAT E 4 .   ? -56.109 12.525  -8.332  1.00 39.60  ? 301 A1EAT B C2M  1 
HETATM 3648 C  C3M  . A1EAT E 4 .   ? -55.096 13.717  -8.262  1.00 37.89  ? 301 A1EAT B C3M  1 
HETATM 3649 C  C4M  . A1EAT E 4 .   ? -55.556 14.917  -9.106  1.00 39.17  ? 301 A1EAT B C4M  1 
HETATM 3650 C  C5M  . A1EAT E 4 .   ? -57.083 15.232  -8.982  1.00 40.14  ? 301 A1EAT B C5M  1 
HETATM 3651 C  C6M  . A1EAT E 4 .   ? -57.610 16.290  -9.932  1.00 37.62  ? 301 A1EAT B C6M  1 
HETATM 3652 O  O2M  . A1EAT E 4 .   ? -56.170 11.950  -9.643  1.00 40.37  ? 301 A1EAT B O2M  1 
HETATM 3653 O  O3M  . A1EAT E 4 .   ? -53.747 13.317  -8.620  1.00 36.89  ? 301 A1EAT B O3M  1 
HETATM 3654 O  O4M  . A1EAT E 4 .   ? -54.806 16.046  -8.653  1.00 39.92  ? 301 A1EAT B O4M  1 
HETATM 3655 O  O5M  . A1EAT E 4 .   ? -57.853 13.993  -9.121  1.00 41.35  ? 301 A1EAT B O5M  1 
HETATM 3656 O  O6M  . A1EAT E 4 .   ? -57.664 15.734  -11.246 1.00 37.05  ? 301 A1EAT B O6M  1 
HETATM 3657 C  C25  . A1EAT E 4 .   ? -53.245 7.244   7.312   1.00 47.27  ? 301 A1EAT B C25  1 
HETATM 3658 N  N3   . A1EAT E 4 .   ? -53.369 8.499   6.578   1.00 46.35  ? 301 A1EAT B N3   1 
HETATM 3659 C  C32  . A1EAT E 4 .   ? -53.017 7.447   8.819   1.00 46.25  ? 301 A1EAT B C32  1 
HETATM 3660 O  O1M2 . A1EAT E 4 .   ? -51.606 7.661   9.047   1.00 46.52  ? 301 A1EAT B O1M2 1 
HETATM 3661 C  C1M2 . A1EAT E 4 .   ? -51.313 8.002   10.407  1.00 47.61  ? 301 A1EAT B C1M2 1 
HETATM 3662 C  C2M2 . A1EAT E 4 .   ? -49.866 8.410   10.507  1.00 41.80  ? 301 A1EAT B C2M2 1 
HETATM 3663 C  C3M2 . A1EAT E 4 .   ? -48.963 7.208   10.233  1.00 44.47  ? 301 A1EAT B C3M2 1 
HETATM 3664 C  C4M2 . A1EAT E 4 .   ? -49.396 5.982   11.061  1.00 44.62  ? 301 A1EAT B C4M2 1 
HETATM 3665 C  C5M2 . A1EAT E 4 .   ? -50.910 5.714   11.022  1.00 43.74  ? 301 A1EAT B C5M2 1 
HETATM 3666 C  C6M2 . A1EAT E 4 .   ? -51.370 4.578   11.918  1.00 41.13  ? 301 A1EAT B C6M2 1 
HETATM 3667 O  O2M2 . A1EAT E 4 .   ? -49.689 8.888   11.826  1.00 43.19  ? 301 A1EAT B O2M2 1 
HETATM 3668 O  O3M2 . A1EAT E 4 .   ? -47.570 7.542   10.415  1.00 38.86  ? 301 A1EAT B O3M2 1 
HETATM 3669 O  O4M2 . A1EAT E 4 .   ? -48.783 4.852   10.480  1.00 45.72  ? 301 A1EAT B O4M2 1 
HETATM 3670 O  O5M2 . A1EAT E 4 .   ? -51.599 6.920   11.330  1.00 47.56  ? 301 A1EAT B O5M2 1 
HETATM 3671 O  O6M2 . A1EAT E 4 .   ? -51.315 4.949   13.287  1.00 43.25  ? 301 A1EAT B O6M2 1 
HETATM 3672 MN MN   . MN    F 2 .   ? -42.607 -2.136  8.386   1.00 47.54  ? 302 MN    B MN   1 
HETATM 3673 CA CA   . CA    G 3 .   ? -45.806 0.291   9.442   1.00 50.08  ? 303 CA    B CA   1 
HETATM 3674 O  O    . HOH   H 5 .   ? -10.773 -53.161 16.665  1.00 72.17  ? 401 HOH   A O    1 
HETATM 3675 O  O    . HOH   H 5 .   ? -29.478 -41.226 21.098  1.00 38.14  ? 402 HOH   A O    1 
HETATM 3676 O  O    . HOH   H 5 .   ? -11.593 -33.254 5.648   1.00 39.77  ? 403 HOH   A O    1 
HETATM 3677 O  O    . HOH   H 5 .   ? -11.399 -35.659 7.546   1.00 38.02  ? 404 HOH   A O    1 
HETATM 3678 O  O    . HOH   H 5 .   ? -8.896  -37.497 8.279   1.00 37.25  ? 405 HOH   A O    1 
HETATM 3679 O  O    . HOH   H 5 .   ? -4.805  -41.774 3.890   1.00 44.38  ? 406 HOH   A O    1 
HETATM 3680 O  O    . HOH   H 5 .   ? -6.043  -37.021 9.952   1.00 34.42  ? 407 HOH   A O    1 
HETATM 3681 O  O    . HOH   H 5 .   ? -15.087 -43.791 31.926  1.00 42.28  ? 408 HOH   A O    1 
HETATM 3682 O  O    . HOH   H 5 .   ? -15.562 -47.068 22.927  1.00 42.59  ? 409 HOH   A O    1 
HETATM 3683 O  O    . HOH   I 5 .   ? -41.407 -0.508  8.740   1.00 35.22  ? 401 HOH   B O    1 
HETATM 3684 O  O    . HOH   I 5 .   ? -40.915 -3.012  7.055   1.00 49.30  ? 402 HOH   B O    1 
HETATM 3685 O  O    . HOH   I 5 .   ? -48.559 6.459   5.353   1.00 43.71  ? 403 HOH   B O    1 
HETATM 3686 O  O    . HOH   I 5 .   ? -46.424 1.125   11.473  1.00 45.08  ? 404 HOH   B O    1 
HETATM 3687 O  O    . HOH   I 5 .   ? -43.851 1.373   9.535   1.00 36.32  ? 405 HOH   B O    1 
HETATM 3688 O  O    . HOH   I 5 .   ? -32.833 10.280  27.678  1.00 50.15  ? 406 HOH   B O    1 
# 
